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Protein

Gag-Pol polyprotein

Gene

gag-pol

Organism
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Gag-Pol polyprotein: Mediates, with Gag polyrotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shutt off translation.
Matrix protein p17: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity).By similarity
Capsid protein p24: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion (PubMed:8648689). Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (PubMed:12660176). Host restriction factors such as monkey TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (PubMed:23785198). Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (PubMed:24554657).By similarity4 Publications
Nucleocapsid protein p7: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly.5 Publications
Protease: Aspartyl protease that mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane (PubMed:9573231, PubMed:11932404). Cleavages take place as an ordered, step-wise cascade to yield mature proteins (PubMed:9573231, PubMed:11932404). This process is called maturation (PubMed:9573231, PubMed:11932404). Displays maximal activity during the budding process just prior to particle release from the cell (PubMed:9573231, PubMed:11932404). Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles (PubMed:7835426). Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (PubMed:12660176, PubMed:19914170).PROSITE-ProRule annotationBy similarity3 Publications
Reverse transcriptase/ribonuclease H: Multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends.1 Publication
Integrase: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration.2 Publications

Catalytic activityi

Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.PROSITE-ProRule annotation
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).PROSITE-ProRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 2 magnesium ions for reverse transcriptase polymerase activity.By similarity
  • Mg2+By similarityNote: Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding.By similarity
  • Mg2+By similarityNote: Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions.By similarity

Enzyme regulationi

Protease: The viral protease is inhibited by many synthetic protease inhibitors (PIs), such as amprenavir, atazanavir, indinavir, loprinavir, nelfinavir, ritonavir and saquinavir. Use of protease inhibitors in tritherapy regimens permit more ambitious therapeutic strategies. Reverse transcriptase/ribonuclease H: RT can be inhibited either by nucleoside RT inhibitors (NRTIs) or by non nucleoside RT inhibitors (NNRTIs). NRTIs act as chain terminators, whereas NNRTIs inhibit DNA polymerization by binding a small hydrophobic pocket near the RT active site and inducing an allosteric change in this region. Classical NRTIs are abacavir, adefovir (PMEA), didanosine (ddI), lamivudine (3TC), stavudine (d4T), tenofovir (PMPA), zalcitabine (ddC), and zidovudine (AZT). Classical NNRTIs are atevirdine (BHAP U-87201E), delavirdine, efavirenz (DMP-266), emivirine (I-EBU), and nevirapine (BI-RG-587). The tritherapies used as a basic effective treatment of AIDS associate two NRTIs and one NNRTI.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei221 – 222Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA2
Active sitei513For protease activity; shared with dimeric partnerPROSITE-ProRule annotation1
Metal bindingi697Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi772Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi773Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Sitei988Essential for RT p66/p51 heterodimerizationBy similarity1
Sitei1001Essential for RT p66/p51 heterodimerizationBy similarity1
Metal bindingi1030Magnesium; catalytic; for RNase H activity1
Metal bindingi1065Magnesium; catalytic; for RNase H activity1 Publication1
Metal bindingi1085Magnesium; catalytic; for RNase H activity1
Metal bindingi1136Magnesium; catalytic; for RNase H activity1 Publication1
Metal bindingi1211Magnesium; catalytic; for integrase activityBy similarity1
Metal bindingi1263Magnesium; catalytic; for integrase activityBy similarity1
Metal bindingi1299Magnesium; catalytic; for integrase activityCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri390 – 407CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri411 – 428CCHC-type 2PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1150 – 1191Integrase-typePROSITE-ProRule annotationAdd BLAST42
DNA bindingi1370 – 1417Integrase-typePROSITE-ProRule annotationAdd BLAST48

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed DNA polymerase, Transferase

Keywords - Biological processi

Activation of host caspases by virus, DNA integration, DNA recombination, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Modulation of host cell apoptosis by virus, Viral genome integration, Viral penetration into host nucleus, Virion maturation, Virus entry into host cell, Virus exit from host cell

Keywords - Ligandi

DNA-binding, Lipid-binding, Magnesium, Metal-binding, RNA-binding, Viral nucleoprotein, Zinc

Enzyme and pathway databases

BRENDAi2.7.7.49. 2676.
3.4.23.16. 2676.
ReactomeiR-HSA-162585. Uncoating of the HIV Virion.
R-HSA-162588. Budding and maturation of HIV virion.
R-HSA-162592. Integration of provirus.
R-HSA-162594. Early Phase of HIV Life Cycle.
R-HSA-164516. Minus-strand DNA synthesis.
R-HSA-164525. Plus-strand DNA synthesis.
R-HSA-164843. 2-LTR circle formation.
R-HSA-173107. Binding and entry of HIV virion.
R-HSA-175474. Assembly Of The HIV Virion.
R-HSA-175567. Integration of viral DNA into host genomic DNA.
R-HSA-177539. Autointegration results in viral DNA circles.
R-HSA-180689. APOBEC3G mediated resistance to HIV-1 infection.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
SABIO-RKP04585.

Names & Taxonomyi

Protein namesi
Recommended name:
Gag-Pol polyprotein
Alternative name(s):
Pr160Gag-Pol
Cleaved into the following 11 chains:
Matrix protein p17
Short name:
MA
Capsid protein p24
Short name:
CA
Spacer peptide 1By similarity
Short name:
SP1
Alternative name(s):
p2
Transframe peptide
Short name:
TF
p6-pol
Short name:
p6*
Alternative name(s):
PR
Retropepsin
Alternative name(s):
Exoribonuclease H (EC:3.1.13.2)
p66 RT
Integrase (EC:2.7.7.-1 Publication, EC:3.1.-.-1 Publication)
Short name:
IN
Gene namesi
Name:gag-pol
OrganismiHuman immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Taxonomic identifieri11706 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000002241 Componenti: Genome

Subcellular locationi

Gag-Pol polyprotein :
  • Host cell membrane; Lipid-anchor By similarity
  • Host endosomehost multivesicular body By similarity

  • Note: These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly.By similarity
Integrase :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cell membrane, Host cytoplasm, Host endosome, Host membrane, Host nucleus, Membrane, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi6S → D: No influence on the PIP2- or concentration-dependent myristyl switch mechanism. 1 Publication1
Mutagenesisi9S → D: No influence on the PIP2- or concentration-dependent myristyl switch mechanism. 1 Publication1
Mutagenesisi18K → A: Replication-defective, induces nuclear mislocalization of matrix protein; when associated with G-22. 1 Publication1
Mutagenesisi22R → G: Replication-defective, induces nuclear mislocalization of matrix protein; when associated with A-18. 1 Publication1
Mutagenesisi27K → A: No effect on subcellular localization of matrix protein; when associated with A-18 and G-22. 1 Publication1
Mutagenesisi67S → D: No influence on the PIP2- or concentration-dependent myristyl switch mechanism. 1 Publication1
Mutagenesisi72S → D: No influence on the PIP2- or concentration-dependent myristyl switch mechanism. 1 Publication1
Mutagenesisi217P → A: 3-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi218V → A: 2.7-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi219H → A or Q: 8-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi220A → G: 44-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi220A → V: 3.4-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi221G → A: 31-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi221G → V: 154-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi222P → A: 36-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi222P → V: More than 150-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi223I → A: 1.2-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi223I → V: 1.0-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi224A → G: 2.3-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi224A → V: 1.7-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi225P → A: 1.6-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi394N → F or G: Decreases infectivity and replication. 1 Publication1
Mutagenesisi400H → C: Complete loss of infectivity and in vitro chaperone activity. 1 Publication1
Mutagenesisi405C → H: Complete loss of infectivity and DNA synthesis. 1 Publication1
Mutagenesisi421H → C: Partial loss of infectivity. Complete loss of in vitro chaperone activity. 1 Publication1
Mutagenesisi426C → H: Partial loss of infectivity. 1 Publication1
Mutagenesisi1065E → Q: Complete loss of RNase H activity. 1 Publication1
Mutagenesisi1136D → N: Complete loss of RNase H activity. 1 Publication1
Mutagenesisi1159H → C: No effect on integrase activity in vitro. 1 Publication1
Mutagenesisi1163H → C or V: 75% increase of integrase activity in vitro. 1 Publication1
Mutagenesisi1187C → A: Complete loss of integrase activity in vivo. 1 Publication1
Mutagenesisi1190C → A: Complete loss of integrase activity in vivo. 1 Publication1
Mutagenesisi1200Q → C: 75% increase of integrase activity in vitro. 1 Publication1
Mutagenesisi1208W → A: Complete loss of integrase activity in vivo. 1 Publication1
Mutagenesisi1211D → A or V: Complete loss of integrase activity in vivo and in vitro. 3 Publications1
Mutagenesisi1213T → A: No effect on infectivity. 1 Publication1
Mutagenesisi1222V → P: Complete loss of integrase activity. 1 Publication1
Mutagenesisi1228S → A: Complete loss of integrase activity in vivo. 2 Publications1
Mutagenesisi1228S → R: No effect on integrase activity in vitro. 2 Publications1
Mutagenesisi1262T → A: No effect infectivity. 1 Publication1
Mutagenesisi1263D → A or I: Complete loss of integrase activity in vivo and in vitro. 3 Publications1
Mutagenesisi1270G → A: No effect on infectivity. 1 Publication1
Mutagenesisi1282I → P: Complete loss of integrase activity in vivo. 1 Publication1
Mutagenesisi1298V → A: No effect on infectivity. 1 Publication1
Mutagenesisi1299E → G or P: Complete loss of integrase activity in vitro. 3 Publications1
Mutagenesisi1306K → P: Slow down virus replication. 1 Publication1
Mutagenesisi1326A → P: Complete loss of integrase activity in vivo. 1 Publication1
Mutagenesisi1346R → C: 75% increase of integrase activity in vitro. 1 Publication1
Mutagenesisi1382W → A: Complete loss of infectivity. No effect on integrase activity in vitro. 2 Publications1
Mutagenesisi1382W → E: 75% increase of integrase activity in vitro. 2 Publications1

Keywords - Diseasei

AIDS

Chemistry databases

ChEMBLiCHEMBL3638360.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00002236202 – 1435Gag-Pol polyproteinAdd BLAST1434
ChainiPRO_00000424392 – 132Matrix protein p17By similarityAdd BLAST131
ChainiPRO_0000042440133 – 363Capsid protein p24By similarityAdd BLAST231
PeptideiPRO_0000042441364 – 377Spacer peptide 1By similarityAdd BLAST14
ChainiPRO_0000042442378 – 432Nucleocapsid protein p7By similarityAdd BLAST55
PeptideiPRO_0000246716433 – 440Transframe peptideSequence analysis8
ChainiPRO_0000042443441 – 488p6-polSequence analysisAdd BLAST48
ChainiPRO_0000038665489 – 587ProteaseAdd BLAST99
ChainiPRO_0000042444588 – 1147Reverse transcriptase/ribonuclease HAdd BLAST560
ChainiPRO_0000042445588 – 1027p51 RTAdd BLAST440
ChainiPRO_00000424461028 – 1147p15Add BLAST120
ChainiPRO_00000424471148 – 1435IntegraseBy similarityAdd BLAST288

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1
Modified residuei132Phosphotyrosine; by hostBy similarity1

Post-translational modificationi

Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. Nucleocapsid protein p7 might be further cleaved after virus entry.PROSITE-ProRule annotation3 Publications
Matrix protein p17: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association (PubMed:17656588).1 Publication
Capsid protein p24: Phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating.By similarity
Nucleocapsid protein p7: Methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei132 – 133Cleavage; by viral proteaseBy similarity2
Sitei363 – 364Cleavage; by viral proteaseBy similarity2
Sitei377 – 378Cleavage; by viral proteaseBy similarity2
Sitei393 – 394Cleavage; by viral proteaseSequence analysis2
Sitei426 – 427Cleavage; by viral proteaseSequence analysis2
Sitei432 – 433Cleavage; by viral proteaseSequence analysis2
Sitei440 – 441Cleavage; by viral proteaseBy similarity2
Sitei488 – 489Cleavage; by viral proteaseBy similarity2
Sitei587 – 588Cleavage; by viral proteaseBy similarity2
Sitei1027 – 1028Cleavage; by viral protease; partialBy similarity2
Sitei1147 – 1148Cleavage; by viral proteaseBy similarity2

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

Matrix protein p17: Homotrimer; further assembles as hexamers of trimers (PubMed:19327811). Matrix protein p17: Interacts with gp41 (via C-terminus) (By similarity). Matrix protein p17: interacts with host CALM1; this interaction induces a conformational change in the Matrix protein, triggering exposure of the myristate group (PubMed:24500712). Matrix protein p17: interacts with host AP3D1; this interaction allows the polyprotein trafficking to multivesicular bodies during virus assembly (By similarity). Matrix protein p17: Part of the pre-integration complex (PIC) which is composed of viral genome, matrix protein, Vpr and integrase (By similarity). Capsid protein p24: Homodimer; the homodimer further multimerizes as homohexamers or homopentamers (PubMed:19914170). Capsid protein p24: Interacts with human PPIA/CYPA (PubMed:9223641); this interaction stabilizes the capsid. Capsid protein p24: Interacts with human NUP153 (By similarity). Capsid protein p24: Interacts with host PDZD8; this interaction stabilizes the capsid (PubMed:20573829). Capsid protein p24: Interacts with monkey TRIM5; this interaction destabilizes the capsid (PubMed:23785198). Protease: Homodimer, whose active site consists of two apposed aspartic acid residues (PubMed:2162350, PubMed:24132393). Reverse transcriptase/ribonuclease H: Heterodimer of p66 RT and p51 RT (RT p66/p51). Heterodimerization of RT is essential for DNA polymerase activity. Despite the sequence identities, p66 RT and p51 RT have distinct folding. Integrase: Homodimer; possibly can form homotetramer. Integrase: Part of the pre-integration complex (PIC) which is composed of viral genome, matrix protein, Vpr and integrase. Integrase: Interacts with human SMARCB1/INI1 and human PSIP1/LEDGF isoform 1 (PubMed:7801128). Integrase: Interacts with human KPNA3; this interaction might play a role in nuclear import of the pre-integration complex (PubMed:19914170). Integrase: Interacts with human NUP153; this interaction might play a role in nuclear import of the pre-integration complex (By similarity).By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself29EBI-3989067,EBI-3989067
KPNA4O006294EBI-9872653,EBI-396343From a different organism.
PSIP1O7547521EBI-3989067,EBI-1801773From a different organism.
PSIP1O75475-12EBI-9872653,EBI-5279836From a different organism.
revP697188EBI-3989067,EBI-8540156From a different organism.
SMARCB1Q128243EBI-9872653,EBI-358419From a different organism.
TNPO3Q9Y5L06EBI-9872653,EBI-1042571From a different organism.

GO - Molecular functioni

  • identical protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi1205538. 127 interactors.
IntActiP04585. 6 interactors.
MINTiMINT-111862.

Chemistry databases

BindingDBiP04585.

Structurei

Secondary structure

11435
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 10Combined sources4
Helixi11 – 18Combined sources8
Beta strandi19 – 21Combined sources3
Beta strandi23 – 25Combined sources3
Helixi31 – 45Combined sources15
Beta strandi46 – 48Combined sources3
Turni50 – 52Combined sources3
Helixi54 – 67Combined sources14
Turni68 – 70Combined sources3
Helixi72 – 90Combined sources19
Helixi97 – 108Combined sources12
Helixi109 – 112Combined sources4
Beta strandi116 – 118Combined sources3
Helixi282 – 284Combined sources3
Helixi293 – 304Combined sources12
Helixi311 – 324Combined sources14
Helixi330 – 337Combined sources8
Helixi343 – 349Combined sources7
Turni350 – 353Combined sources4
Beta strandi357 – 360Combined sources4
Beta strandi393 – 395Combined sources3
Turni402 – 404Combined sources3
Beta strandi414 – 416Combined sources3
Turni423 – 425Combined sources3
Beta strandi485 – 487Combined sources3
Beta strandi491 – 495Combined sources5
Beta strandi498 – 503Combined sources6
Beta strandi506 – 512Combined sources7
Beta strandi517 – 521Combined sources5
Beta strandi530 – 537Combined sources8
Beta strandi540 – 554Combined sources15
Beta strandi557 – 566Combined sources10
Beta strandi569 – 573Combined sources5
Helixi575 – 578Combined sources4
Helixi579 – 581Combined sources3
Beta strandi584 – 586Combined sources3
Beta strandi599 – 602Combined sources4
Helixi615 – 630Combined sources16
Beta strandi633 – 636Combined sources4
Beta strandi639 – 641Combined sources3
Beta strandi647 – 651Combined sources5
Turni653 – 656Combined sources4
Beta strandi658 – 662Combined sources5
Helixi665 – 670Combined sources6
Helixi672 – 676Combined sources5
Turni677 – 679Combined sources3
Helixi684 – 686Combined sources3
Helixi687 – 689Combined sources3
Beta strandi691 – 697Combined sources7
Turni699 – 701Combined sources3
Helixi702 – 704Combined sources3
Beta strandi705 – 707Combined sources3
Helixi709 – 715Combined sources7
Beta strandi717 – 719Combined sources3
Helixi722 – 724Combined sources3
Beta strandi725 – 727Combined sources3
Beta strandi729 – 735Combined sources7
Helixi743 – 761Combined sources19
Beta strandi762 – 765Combined sources4
Beta strandi766 – 770Combined sources5
Beta strandi773 – 778Combined sources6
Helixi782 – 798Combined sources17
Helixi806 – 808Combined sources3
Beta strandi812 – 816Combined sources5
Beta strandi819 – 821Combined sources3
Helixi823 – 825Combined sources3
Beta strandi826 – 828Combined sources3
Beta strandi837 – 840Combined sources4
Helixi841 – 854Combined sources14
Turni855 – 857Combined sources3
Beta strandi858 – 860Combined sources3
Helixi864 – 869Combined sources6
Turni870 – 872Combined sources3
Beta strandi876 – 879Combined sources4
Helixi884 – 896Combined sources13
Beta strandi902 – 904Combined sources3
Beta strandi908 – 910Combined sources3
Beta strandi913 – 918Combined sources6
Beta strandi920 – 922Combined sources3
Beta strandi924 – 931Combined sources8
Beta strandi935 – 941Combined sources7
Beta strandi945 – 949Combined sources5
Helixi951 – 970Combined sources20
Beta strandi975 – 980Combined sources6
Helixi982 – 991Combined sources10
Beta strandi992 – 995Combined sources4
Beta strandi1000 – 1003Combined sources4
Helixi1008 – 1013Combined sources6
Beta strandi1024 – 1033Combined sources10
Turni1035 – 1037Combined sources3
Beta strandi1039 – 1046Combined sources8
Beta strandi1047 – 1049Combined sources3
Beta strandi1051 – 1058Combined sources8
Helixi1061 – 1074Combined sources14
Beta strandi1078 – 1084Combined sources7
Helixi1087 – 1094Combined sources8
Beta strandi1098 – 1102Combined sources5
Helixi1103 – 1114Combined sources12
Beta strandi1116 – 1122Combined sources7
Beta strandi1125 – 1127Combined sources3
Helixi1130 – 1139Combined sources10
Turni1140 – 1142Combined sources3
Helixi1204 – 1206Combined sources3
Beta strandi1207 – 1215Combined sources9
Beta strandi1218 – 1225Combined sources8
Turni1226 – 1228Combined sources3
Beta strandi1231 – 1240Combined sources10
Helixi1241 – 1254Combined sources14
Beta strandi1259 – 1261Combined sources3
Helixi1266 – 1268Combined sources3
Helixi1271 – 1280Combined sources10
Helixi1302 – 1312Combined sources11
Helixi1313 – 1315Combined sources3
Helixi1319 – 1332Combined sources14
Beta strandi1335 – 1339Combined sources5
Helixi1343 – 1355Combined sources13
Helixi1358 – 1368Combined sources11
Beta strandi1370 – 1374Combined sources5
Beta strandi1383 – 1391Combined sources9
Beta strandi1393 – 1399Combined sources7
Beta strandi1404 – 1408Combined sources5
Helixi1409 – 1411Combined sources3
Beta strandi1412 – 1414Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A30X-ray2.00A/B489-587[»]
1BV7X-ray2.00A/B489-587[»]
1BV9X-ray2.00A/B489-587[»]
1BVENMR-A/B489-587[»]
1BVGNMR-A/B489-587[»]
1BWAX-ray1.90A/B489-587[»]
1BWBX-ray1.80A/B489-587[»]
1C0TX-ray2.70A588-1147[»]
B588-1027[»]
1C0UX-ray2.52A588-1147[»]
B588-1027[»]
1C1BX-ray2.50A588-1147[»]
B588-1428[»]
1C1CX-ray2.50A588-1147[»]
B588-1027[»]
1DMPX-ray2.00A/B489-587[»]
1DTQX-ray2.80A588-1147[»]
B588-1027[»]
1DTTX-ray3.00A588-1147[»]
B588-1027[»]
1E6JX-ray3.00P143-352[»]
1EP4X-ray2.50A588-1147[»]
B588-1027[»]
1ESKNMR-A390-430[»]
1EX4X-ray2.80A/B1199-1435[»]
1EXQX-ray1.60A/B1203-1356[»]
1FB7X-ray2.60A489-587[»]
1FK9X-ray2.50A588-1130[»]
B588-1027[»]
1FKOX-ray2.90A588-1130[»]
B588-1027[»]
1FKPX-ray2.90A588-1130[»]
B588-1027[»]
1G6LX-ray1.90A484-587[»]
1HIVX-ray2.00A/B489-587[»]
1HVHX-ray1.80A/B489-587[»]
1HVRX-ray1.80A/B489-587[»]
1HWRX-ray1.80A/B489-587[»]
1HXBX-ray2.30A/B489-587[»]
1JKHX-ray2.50A588-1147[»]
B588-1027[»]
1JLAX-ray2.50A588-1147[»]
B588-1027[»]
1JLBX-ray3.00A588-1147[»]
B588-1027[»]
1JLCX-ray3.00A588-1147[»]
B588-1027[»]
1JLEX-ray2.80A588-1147[»]
B588-1027[»]
1JLFX-ray2.60A588-1147[»]
B588-1027[»]
1JLGX-ray2.60A588-1147[»]
B588-1027[»]
1JLQX-ray3.00A588-1147[»]
B588-1027[»]
1KLMX-ray2.65A588-1147[»]
B588-1027[»]
1LV1X-ray2.10A484-587[»]
1LW0X-ray2.80A588-1147[»]
B588-1027[»]
1LW2X-ray3.00A588-1147[»]
B588-1027[»]
1LWCX-ray2.62A588-1147[»]
B588-1027[»]
1LWEX-ray2.81A588-1147[»]
B588-1027[»]
1LWFX-ray2.80A588-1147[»]
B588-1027[»]
1NCPNMR-N390-406[»]
1O1WNMR-A1014-1147[»]
1ODWX-ray2.10A/B489-587[»]
1ODYX-ray2.00A/B489-587[»]
1QBRX-ray1.80A/B489-587[»]
1QBSX-ray1.80A/B489-587[»]
1QBTX-ray2.10A/B489-587[»]
1QBUX-ray1.80A/B489-587[»]
1REVX-ray2.60A588-1147[»]
B588-1027[»]
1RT1X-ray2.55A588-1147[»]
B588-1027[»]
1RT2X-ray2.55A588-1147[»]
B588-1027[»]
1RT3X-ray3.00A588-1147[»]
B588-1027[»]
1RT4X-ray2.90A588-1147[»]
B588-1027[»]
1RT5X-ray2.90A588-1147[»]
B588-1027[»]
1RT6X-ray2.80A588-1147[»]
B588-1027[»]
1RT7X-ray3.00A588-1147[»]
B588-1027[»]
1RTDX-ray3.20B/D588-1027[»]
1RTHX-ray2.20A588-1147[»]
B588-1027[»]
1RTIX-ray3.00A588-1147[»]
B588-1027[»]
1RTJX-ray2.35A588-1147[»]
B588-1027[»]
1S1TX-ray2.40A588-1147[»]
B588-1027[»]
1S1UX-ray3.00A588-1147[»]
B588-1027[»]
1S1VX-ray2.60A588-1147[»]
B588-1027[»]
1S1WX-ray2.70A588-1147[»]
B588-1027[»]
1S1XX-ray2.80A588-1147[»]
B588-1027[»]
1T05X-ray3.00B588-1016[»]
1TAMNMR-A1-132[»]
1TKTX-ray2.60A588-1147[»]
B588-1027[»]
1TKXX-ray2.85A588-1147[»]
B588-1027[»]
1TKZX-ray2.81A588-1147[»]
B588-1027[»]
1TL1X-ray2.90A588-1147[»]
B588-1027[»]
1TL3X-ray2.80A588-1147[»]
B588-1027[»]
1VRTX-ray2.20A588-1147[»]
B588-1027[»]
1VRUX-ray2.40A588-1147[»]
B588-1027[»]
2HNDX-ray2.50A591-1124[»]
2HNYX-ray2.50A591-1124[»]
2HNZX-ray3.00A591-1124[»]
B594-1015[»]
2KODNMR-A/B276-363[»]
2NPHX-ray1.65A/B489-587[»]
2OPPX-ray2.55A591-1132[»]
B592-1018[»]
2OPQX-ray2.80A591-1124[»]
B592-1015[»]
2OPRX-ray2.90A589-1135[»]
B593-1018[»]
2OPSX-ray2.30A589-1130[»]
B593-1027[»]
2RF2X-ray2.40A588-1147[»]
B588-1027[»]
2RKIX-ray2.30A588-1147[»]
B588-1027[»]
2WHHX-ray1.69A489-587[»]
2WOMX-ray3.20A588-1147[»]
B588-1027[»]
2WONX-ray2.80A588-1147[»]
B588-1027[»]
2YNFX-ray2.36A588-1147[»]
B588-1015[»]
2YNGX-ray2.12A588-1147[»]
B588-1015[»]
2YNHX-ray2.90A588-1147[»]
B588-1015[»]
2YNIX-ray2.49A588-1147[»]
B588-1015[»]
3AO2X-ray1.80A/B1197-1359[»]
3C6TX-ray2.70A588-1147[»]
B588-1027[»]
3C6UX-ray2.70A588-1147[»]
B588-1027[»]
3DI6X-ray2.65A588-1148[»]
B588-1027[»]
3DLEX-ray2.50A588-1147[»]
B588-1027[»]
3DLGX-ray2.20A588-1147[»]
B588-1027[»]
3DM2X-ray3.10A588-1147[»]
B588-1027[»]
3DMJX-ray2.60A588-1147[»]
B588-1027[»]
3DOKX-ray2.90A588-1147[»]
B588-1027[»]
3DOLX-ray2.50A588-1147[»]
B588-1027[»]
3DOXX-ray2.00A484-587[»]
3DRPX-ray2.60A588-1147[»]
B588-1027[»]
3DRRX-ray2.89A588-1147[»]
B588-1027[»]
3DRSX-ray3.15A588-1147[»]
B588-1027[»]
3DYAX-ray2.30A588-1148[»]
B588-1027[»]
3E01X-ray2.95A588-1148[»]
B588-1027[»]
3FFIX-ray2.60A588-1147[»]
B588-1027[»]
3I0RX-ray2.98A588-1147[»]
B588-1027[»]
3I0SX-ray2.70A588-1147[»]
B588-1027[»]
3KJVX-ray3.10A588-1147[»]
B588-1027[»]
3KK1X-ray2.70A588-1147[»]
B588-1027[»]
3KK2X-ray2.90A588-1147[»]
B588-1027[»]
3KK3X-ray2.90A588-1147[»]
B588-1027[»]
3KT2X-ray1.65A484-587[»]
3KT5X-ray1.80A484-587[»]
3LAKX-ray2.30A/B588-1147[»]
3LALX-ray2.51A/B588-1147[»]
3LAMX-ray2.76A/B588-1147[»]
3LANX-ray2.55A/B588-1147[»]
3LP0X-ray2.79A588-1147[»]
B588-1027[»]
3LP1X-ray2.23A588-1147[»]
B588-1027[»]
3LP2X-ray2.80A588-1147[»]
B588-1027[»]
3M8PX-ray2.67A588-1148[»]
B588-1027[»]
3M8QX-ray2.70A588-1148[»]
B588-1027[»]
3MECX-ray2.30A588-1147[»]
B588-1027[»]
3MEDX-ray2.50A588-1147[»]
B588-1027[»]
3MEEX-ray2.40A588-1147[»]
B588-1027[»]
3MEGX-ray2.80A588-1147[»]
B588-1027[»]
3MIMX-ray1.76A/B489-587[»]
3N3IX-ray2.50A484-587[»]
3NBPX-ray2.95A588-1148[»]
B588-1027[»]
3PHVX-ray2.70A489-587[»]
3QINX-ray1.70A1014-1103[»]
A1142-1148[»]
3QIOX-ray1.40A1014-1148[»]
3QIPX-ray2.09A588-1147[»]
B588-1027[»]
3T19X-ray2.60A/B588-1147[»]
3T1AX-ray2.40A/B588-1147[»]
3TAMX-ray2.51A590-1147[»]
B588-1027[»]
4B3OX-ray3.30A588-1145[»]
B588-1027[»]
4B3PX-ray4.84A588-1145[»]
B588-1027[»]
4B3QX-ray5.00A588-1145[»]
B588-1027[»]
4I7FX-ray2.50A588-1147[»]
B588-1027[»]
4KSEX-ray2.68B588-1017[»]
4KV8X-ray2.30A588-1147[»]
B588-1027[»]
4NCGX-ray2.58A588-1147[»]
B585-1027[»]
4Q1WX-ray1.85A/B496-587[»]
4Q1XX-ray1.90A/B496-587[»]
4Q1YX-ray1.50A/B496-587[»]
4Q5MX-ray1.79A484-587[»]
4QLHX-ray2.45A489-592[»]
4U1HX-ray1.59C180-188[»]
4U1IX-ray1.92C180-188[»]
4U1JX-ray1.38C180-188[»]
4U7QX-ray1.70A/B496-587[»]
4U7VX-ray1.38A/B496-587[»]
5DGUX-ray1.22A/B496-587[»]
5DGWX-ray1.62A/B496-587[»]
5EU7X-ray2.64A/B1204-1356[»]
5J2MX-ray2.43A588-1147[»]
B588-1027[»]
5J2NX-ray2.90A588-1147[»]
B588-1027[»]
5J2PX-ray2.53A588-1147[»]
B588-1027[»]
5J2QX-ray2.79A588-1147[»]
B588-1027[»]
5K14X-ray2.40A588-1147[»]
ProteinModelPortaliP04585.
SMRiP04585.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04585.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini508 – 577Peptidase A2PROSITE-ProRule annotationAdd BLAST70
Domaini631 – 821Reverse transcriptasePROSITE-ProRule annotationAdd BLAST191
Domaini1021 – 1144RNase HPROSITE-ProRule annotationAdd BLAST124
Domaini1201 – 1351Integrase catalyticPROSITE-ProRule annotationAdd BLAST151

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni7 – 31Interaction with Gp41By similarityAdd BLAST25
Regioni8 – 43Interaction with host CALM11 PublicationAdd BLAST36
Regioni12 – 19Interaction with host AP3D1By similarity8
Regioni14 – 33Interaction with membrane phosphatidylinositol 4,5-bisphosphate and RNABy similarityAdd BLAST20
Regioni73 – 77Interaction with membrane phosphatidylinositol 4,5-bisphosphateBy similarity5
Regioni189 – 227Interaction with host PPIA/CYPA and NUP153By similarityAdd BLAST39
Regioni217 – 225PPIA/CYPA-binding loop9
Regioni277 – 363Dimerization/Multimerization of capsid protein p24Add BLAST87
Regioni489 – 493Dimerization of protease1 Publication5
Regioni537 – 543Dimerization of protease1 Publication7
Regioni576 – 588Dimerization of protease1 PublicationAdd BLAST13
Regioni814 – 822RT 'primer grip'By similarity9

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi16 – 22Nuclear export signalBy similarity7
Motifi26 – 32Nuclear localization signalBy similarity7
Motifi985 – 1001Tryptophan repeat motifBy similarityAdd BLAST17

Domaini

Reverse transcriptase/ribonuclease H: RT is structured in five subdomains: finger, palm, thumb, connection and RNase H. Within the palm subdomain, the 'primer grip' region is thought to be involved in the positioning of the primer terminus for accommodating the incoming nucleotide. The RNase H domain stabilizes the association of RT with primer-template (By similarity).By similarity
Reverse transcriptase/ribonuclease H: The tryptophan repeat motif is involved in RT p66/p51 dimerization.
Integrase: The core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein.

Sequence similaritiesi

Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation
Contains 1 integrase catalytic domain.PROSITE-ProRule annotation
Contains 1 integrase-type DNA-binding domain.PROSITE-ProRule annotation
Contains 1 integrase-type zinc finger.PROSITE-ProRule annotation
Contains 1 peptidase A2 domain.PROSITE-ProRule annotation
Contains 1 reverse transcriptase domain.PROSITE-ProRule annotation
Contains 1 RNase H domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri390 – 407CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri411 – 428CCHC-type 2PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1150 – 1191Integrase-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Repeat, Zinc-finger

Family and domain databases

Gene3Di1.10.10.200. 1 hit.
1.10.1200.30. 1 hit.
1.10.150.90. 1 hit.
1.10.375.10. 1 hit.
2.30.30.10. 1 hit.
2.40.70.10. 1 hit.
3.30.420.10. 2 hits.
4.10.60.10. 1 hit.
InterProiIPR001969. Aspartic_peptidase_AS.
IPR000721. Gag_p24.
IPR001037. Integrase_C_retrovir.
IPR001584. Integrase_cat-core.
IPR017856. Integrase_Zn-bd_dom-like_N.
IPR003308. Integrase_Zn-bd_dom_N.
IPR000071. Lentvrl_matrix_N.
IPR012344. Matrix_HIV/RSV.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR018061. Retropepsins.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR010659. RVT_connect.
IPR010661. RVT_thumb.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00540. Gag_p17. 1 hit.
PF00607. Gag_p24. 1 hit.
PF00552. IN_DBD_C. 1 hit.
PF02022. Integrase_Zn. 1 hit.
PF00075. RNase_H. 1 hit.
PF00665. rve. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
PF06815. RVT_connect. 1 hit.
PF06817. RVT_thumb. 1 hit.
PF00098. zf-CCHC. 2 hits.
[Graphical view]
PRINTSiPR00234. HIV1MATRIX.
SMARTiSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF46919. SSF46919. 1 hit.
SSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF50122. SSF50122. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF53098. SSF53098. 2 hits.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50994. INTEGRASE. 1 hit.
PS51027. INTEGRASE_DBD. 1 hit.
PS50879. RNASE_H. 1 hit.
PS50878. RT_POL. 1 hit.
PS50158. ZF_CCHC. 2 hits.
PS50876. ZF_INTEGRASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by ribosomal frameshifting. AlignAdd to basket

Note: Translation results in the formation of the Gag polyprotein most of the time. Ribosomal frameshifting at the gag-pol genes boundary occurs at low frequency and produces the Gag-Pol polyprotein. This strategy of translation probably allows the virus to modulate the quantity of each viral protein. Maintenance of a correct Gag to Gag-Pol ratio is essential for RNA dimerization and viral infectivity.
Isoform Gag-Pol polyprotein (identifier: P04585-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGARASVLSG GELDRWEKIR LRPGGKKKYK LKHIVWASRE LERFAVNPGL
60 70 80 90 100
LETSEGCRQI LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIEIKDTKEA
110 120 130 140 150
LDKIEEEQNK SKKKAQQAAA DTGHSNQVSQ NYPIVQNIQG QMVHQAISPR
160 170 180 190 200
TLNAWVKVVE EKAFSPEVIP MFSALSEGAT PQDLNTMLNT VGGHQAAMQM
210 220 230 240 250
LKETINEEAA EWDRVHPVHA GPIAPGQMRE PRGSDIAGTT STLQEQIGWM
260 270 280 290 300
TNNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF
310 320 330 340 350
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPA ATLEEMMTAC
360 370 380 390 400
QGVGGPGHKA RVLAEAMSQV TNSATIMMQR GNFRNQRKIV KCFNCGKEGH
410 420 430 440 450
TARNCRAPRK KGCWKCGKEG HQMKDCTERQ ANFLREDLAF LQGKAREFSS
460 470 480 490 500
EQTRANSPTR RELQVWGRDN NSPSEAGADR QGTVSFNFPQ VTLWQRPLVT
510 520 530 540 550
IKIGGQLKEA LLDTGADDTV LEEMSLPGRW KPKMIGGIGG FIKVRQYDQI
560 570 580 590 600
LIEICGHKAI GTVLVGPTPV NIIGRNLLTQ IGCTLNFPIS PIETVPVKLK
610 620 630 640 650
PGMDGPKVKQ WPLTEEKIKA LVEICTEMEK EGKISKIGPE NPYNTPVFAI
660 670 680 690 700
KKKDSTKWRK LVDFRELNKR TQDFWEVQLG IPHPAGLKKK KSVTVLDVGD
710 720 730 740 750
AYFSVPLDED FRKYTAFTIP SINNETPGIR YQYNVLPQGW KGSPAIFQSS
760 770 780 790 800
MTKILEPFRK QNPDIVIYQY MDDLYVGSDL EIGQHRTKIE ELRQHLLRWG
810 820 830 840 850
LTTPDKKHQK EPPFLWMGYE LHPDKWTVQP IVLPEKDSWT VNDIQKLVGK
860 870 880 890 900
LNWASQIYPG IKVRQLCKLL RGTKALTEVI PLTEEAELEL AENREILKEP
910 920 930 940 950
VHGVYYDPSK DLIAEIQKQG QGQWTYQIYQ EPFKNLKTGK YARMRGAHTN
960 970 980 990 1000
DVKQLTEAVQ KITTESIVIW GKTPKFKLPI QKETWETWWT EYWQATWIPE
1010 1020 1030 1040 1050
WEFVNTPPLV KLWYQLEKEP IVGAETFYVD GAANRETKLG KAGYVTNRGR
1060 1070 1080 1090 1100
QKVVTLTDTT NQKTELQAIY LALQDSGLEV NIVTDSQYAL GIIQAQPDQS
1110 1120 1130 1140 1150
ESELVNQIIE QLIKKEKVYL AWVPAHKGIG GNEQVDKLVS AGIRKVLFLD
1160 1170 1180 1190 1200
GIDKAQDEHE KYHSNWRAMA SDFNLPPVVA KEIVASCDKC QLKGEAMHGQ
1210 1220 1230 1240 1250
VDCSPGIWQL DCTHLEGKVI LVAVHVASGY IEAEVIPAET GQETAYFLLK
1260 1270 1280 1290 1300
LAGRWPVKTI HTDNGSNFTG ATVRAACWWA GIKQEFGIPY NPQSQGVVES
1310 1320 1330 1340 1350
MNKELKKIIG QVRDQAEHLK TAVQMAVFIH NFKRKGGIGG YSAGERIVDI
1360 1370 1380 1390 1400
IATDIQTKEL QKQITKIQNF RVYYRDSRNP LWKGPAKLLW KGEGAVVIQD
1410 1420 1430
NSDIKVVPRR KAKIIRDYGK QMAGDDCVAS RQDED
Note: Produced by -1 ribosomal frameshifting.
Length:1,435
Mass (Da):162,042
Last modified:January 23, 2007 - v4
Checksum:i8487B36BDEAC5FE4
GO
Isoform Gag polyprotein (identifier: P04591-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P04591.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.
Length:500
Mass (Da):55,930
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti496R → K Confers to resistance to A-77003; when associated with other amino acid changes. 1
Natural varianti496R → Q Confers to resistance to A-77003. 1
Natural varianti498L → F Confers resistance to amprenavir, atazanavir, lopinavir; when associated with other amino acid changes. 1
Natural varianti498L → I Confers resistance to indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti498L → R Confers resistance to indinavir and lopinavir; when associated with other amino acid changes. 1
Natural varianti498L → V Confers resistance to indinavir and lopinavir; when associated with other amino acid changes. 1
Natural varianti498L → Y Confers resistance to atazanavir; when associated with other amino acid changes. 1
Natural varianti503I → V Confers resistance to tipranavir. 1
Natural varianti504G → E Confers resistance to lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti508K → I Confers resistance to lopinavir. 1
Natural varianti508K → M Confers resistance to indinavir, lopinavir and nelfinavir; when associated with other amino acid changes. 1
Natural varianti508K → R Confers resistance to indinavir, lopinavir and ritonavir; when associated with other amino acid changes. 1
Natural varianti511L → I Confers resistance to BILA 2185 BS. 1
Natural varianti512L → I Confers resistance to amprenavir, indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti518D → N Confers resistance to nelfinavir; when associated with other amino acid changes. 1
Natural varianti520V → I Confers resistance to A-77003, amprenavir, atazanavir, indinavir, kynostatin, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti521L → F Confers resistance to atazanavir nelfinavir and ritonavir; when associated with other amino acid changes. 1
Natural varianti522E → Q Confers resistance to lopinavir; when associated with other amino acid changes. 1
Natural varianti523E → D Confers resistance to tipranavir. 1
Natural varianti524M → I Confers resistance to nelfinavir and ritonavir; when associated with other amino acid changes. 1
Natural varianti524M → L Confers resistance to ritonavir; when associated with other amino acid changes. 1
Natural varianti525S → D Confers resistance to indinavir and tipranavir; when associated with other amino acid changes. 1
Natural varianti529R → K Confers resistance to tipranavir. 1
Natural varianti533K → I Confers resistance to DMD-323; when associated with other amino acid changes. 1
Natural varianti534M → F Confers resistance to A-77003. 1
Natural varianti534M → I Confers resistance to A-77003, amprenavir, atazanavir, indinavir, kynostatin, lopinavir, ritonavir, saquinavir and telinavir; when associated with other amino acid changes. 1
Natural varianti534M → L Confers resistance to A-77003, amprenavir, indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti535I → V Confers resistance to amprenavir, lopinavir, kynostatin, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti536G → V Confers resistance to A-77003, amprenavir, indinavir, ritonavir, saquinavir and telinavir; when associated with other amino acid changes. 1
Natural varianti538I → L Confers resistance to atazanavir; when associated with other amino acid changes. 1
Natural varianti538I → V Confers resistance to amprenavir, lopinavir and ritonavir; when associated with other amino acid changes. 1
Natural varianti541F → L Confers resistance to lopinavir and telinavir; when associated with other amino acid changes. 1
Natural varianti541F → Y Confers resistance to indinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti542I → A Confers resistance to lopinavir. 1
Natural varianti542I → L Confers resistance to amprenavir and lopinavir; when associated with other amino acid changes. 1
Natural varianti542I → M Confers resistance to amprenavir and lopinavir. 1
Natural varianti542I → S Confers resistance to lopinavir. 1
Natural varianti542I → T Confers resistance to lopinavir; when associated with other amino acid changes. 1
Natural varianti542I → V Confers resistance to indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti543K → R Confers resistance to nelfinavir. 1
Natural varianti545R → K Confers resistance to nelfinavir. 1
Natural varianti546Q → E Confers resistance to lopinavir and ritonavir; when associated with other amino acid changes. 1
Natural varianti548D → E Confers resistance to tripanavir. 1
Natural varianti549Q → H Confers resistance to lopinavir; when associated with other amino acid changes. 1
Natural varianti551L → P Confers resistance to atazanavir, indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti551L → T Confers resistance to lopinavir. 1
Natural varianti553E → Q Confers resistance to lopinavir; when associated with other amino acid changes. 1
Natural varianti554I → F Confers resistance to indinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti557H → Y Confers resistance to lopinavir; when associated with other amino acid changes. 1
Natural varianti559A → I Confers resistance to lopinavir; when associated with other amino acid changes. 1
Natural varianti559A → L Confers resistance to lopinavir; when associated with other amino acid changes. 1
Natural varianti559A → T Confers resistance to A-77003, indinavir, lopinavir, nelfinavir and tripanavir; when associated with other amino acid changes. 1
Natural varianti559A → V Confers resistance to amprenavir, atazanavir, indinavir, kynostatin, lopinavir, nelfinavir, ritonavir, saquinavir and telinavir; when associated with other amino acid changes. 1
Natural varianti561G → S Confers resistance to indinavir, nelfinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti565V → I Confers resistance to indinavir, nelfinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti570V → A Confers resistance to A-77003, indinavir, lopinavir, nelfinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti570V → F Confers resistance to lopinavir and ritonavir; when associated with other amino acid changes. 1
Natural varianti570V → I Confers resistance to A-77003 and kynostatin; when associated with other amino acid changes. 1
Natural varianti570V → S Confers resistance to lopinavir and ritonavir. 1
Natural varianti570V → T Confers resistance to indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti572I → A Confers resistance to atazanavir, indinavir, lopinavir, nelfinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti572I → V Confers resistance to amprenavir, atazanavir, indinavir, kynostatin, lopinavir, nelfinavir, ritonavir, saquinavir and telinavir; when associated with other amino acid changes. 1
Natural varianti576N → D Confers resistance to nelfinavir; when associated with other amino acid changes. 1
Natural varianti576N → S Confers resistance to atazanavir, indinavir and nelfinavir; when associated with other amino acid changes. 1
Natural varianti577L → M Confers resistance to atazanavir; when associated with other amino acid changes. 1
Natural varianti578L → M Confers resistance to indinavir, lopinavir, nelfinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti579T → S Confers resistance to lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti581I → L Confers resistance to indinavir. 1
Natural varianti628M → L Confers resistance to zidovudine; when associated with other amino acid changes. 1
Natural varianti631E → A Confers resistance to lamivudine. 1
Natural varianti631E → D Confers resistance to zidovudine; when associated with other amino acid changes. 1
Natural varianti639P → R Confers resistance to stavudine. 1
Natural varianti641N → D Confers resistance to stavudine. 1
Natural varianti649A → V Confers multi-NRTI resistance; when associated with other amino acid changes. 1
Natural varianti652K → R Confers resistance to abacavir, adefovir, didenosine, lamivudine, stavudine, tenofir and zidovuline; when associated with other amino acid changes. 1
Natural varianti654D → A Confers resistance to zidovudine. 1
Natural varianti654D → E Confers multi-NRTI resistance. 1
Natural varianti654D → G Confers multi-NRTI resistance. 1
Natural varianti654D → N Confers resistance to zidovudine. 1
Natural varianti654D → S Confers multi-NRTI resistance. 1
Natural varianti655S → G Confers multi-NRTI resistance; when associated with other amino acid changes. 1
Natural varianti655S → N Confers multi-NRTI resistance. 1
Natural varianti655S → Y Confers multi-NRTI resistance. 1
Natural varianti656T → A Confers resistance to lamivudine and stavudine. 1
Natural varianti656T → D Confers resistance to lamivudine, stavudine and rarely to zalcitabine. 1
Natural varianti656T → G Confers resistance to didanosine, zalcitabine and zidovudine. 1
Natural varianti656T → N Confers resistance to lamivudine and stavudine. 1
Natural varianti657K → E Confers resistance to adefovir and lamivudine. 1
Natural varianti657K → R Confers resistance to zidovudine; when associated with other amino acid changes. 1
Natural varianti657K → S Confers resistance to didanosine and stavudine. 1
Natural varianti661L → I Confers resistance to HBY 097. 1
Natural varianti661L → V Confers resistance to abacavir, didanosine, HBY 097 and zalcitabine; when associated with other amino acid changes. 1
Natural varianti662V → I Confers multi-NRTI resistance; when associated with other amino acid changes. 1
Natural varianti662V → L Confers resistance to HBY 097. 1
Natural varianti662V → M Confers resistance to stavudine and zalcitabine. 1
Natural varianti662V → T Confers resistance to d4C, didanosine, stavudine and zalcitabine. 1
Natural varianti664F → L Confers multi-NRTI resistance; when associated with other amino acid changes. 1
Natural varianti675W → G Confers resistance to pyrophosphate analog PFA. 1
Natural varianti675W → S Confers resistance to pyrophosphate analog PFA. 1
Natural varianti676E → G Confers resistance to pyrophosphate analog PFA. 1
Natural varianti676E → K Confers resistance to pyrophosphate analog PFA. 1
Natural varianti679L → I Confers resistance to pyrophosphate analog PFA. 1
Natural varianti687L → I Confers resistance to nevirapine and efavirenz. 1
Natural varianti688K → E Confers resistance to atevirdine, efavirenz, nevirapine and zidovudine. 1
Natural varianti688K → P Confers resistance to TMC125; when associated with E-142. 1
Natural varianti688K → Q Confers resistance to efavirenz; when associated with I-19. 1
Natural varianti690K → E Confers resistance to atevirdine; when associated with other amino acid changes. 1
Natural varianti690K → N Confers resistance to atevirdine, efavirenz, emivirine and nevirapine; when associated with other amino acid changes. 1
Natural varianti690K → R Confers resistance to emivirine and trovirdine; when associated with other D-179 and C-181. 1
Natural varianti693V → A Confers resistance to nevirapine. 1
Natural varianti693V → I Confers resistance to HBY 097. 1
Natural varianti693V → M Confers resistance to delavirdine, efavirenz and nevirapine. 1
Natural varianti695V → I Confers resistance to efavirenz, emivirine, nevirapine and trovirdine; when associated with other amino acid changes. 1
Natural varianti702Y → F Confers resistance to abacavir; when associated with other amino acid changes. 1
Natural varianti703F → Y Confers multi-NRTI resistance; when associated with other amino acid changes. 1
Natural varianti705V → I Confers resistance to zidovudine; when associated with other amino acid changes. 1
Natural varianti706P → S Confers resistance to lodenosine. 1
Natural varianti722I → L Confers resistance to delavirdine, efavirenz and nevirapine; when associated with I-239. 1
Natural varianti722I → M Confers resistance to delavirdine, efavirenz and nevirapine; when associated with I-239. 1
Natural varianti722I → T Confers resistance to delavirdine, efavirenz and nevirapine; when associated with I-239. 1
Natural varianti725E → K Confers resistance to emivirine. 1
Natural varianti732Q → M Confers both multi-NRTI and multi-NNRTI resistance. 1
Natural varianti738Q → M Confers multi-NRTI resistance; when associated with other amino acid changes. 1
Natural varianti743S → A Confers resistance to pyrophosphate analog PFA. 1
Natural varianti744P → S Confers resistance to lamivudine. 1
Natural varianti748Q → L Confers resistance to pyrophosphate analog PFA. 1
Natural varianti766V → D Confers resistance to efavirenz, tivirapine and trovirdine; when associated with other amino acid changes. 1
Natural varianti768Y → C Confers multi-NNRTI resistance. 1
Natural varianti771M → I Confers resistance to lamivudine and emtricitabine. 1
Natural varianti771M → T Confers resistance to abacavir, didanosine, emtricitabine, lamivudine and zalcitabine. 1
Natural varianti771M → V Confers resistance to lamivudine. 1
Natural varianti775Y → C Confers resistance to nevirapine. 1
Natural varianti775Y → H Confers resistance to atevirdine, efavirenz, loviride and zidovudine. 1
Natural varianti775Y → L Confers resistance to efavirenz. 1
Natural varianti776V → I Confers resistance to HBY 097. 1
Natural varianti777G → A Confers resistance to efavirenz and nevirapine. 1
Natural varianti777G → C Confers resistance to efavirenz and nevirapine. 1
Natural varianti777G → E Confers resistance to efavirenz, nevirapine and quinoxaline. 1
Natural varianti777G → Q Confers resistance to efavirenz, HBY 097 and nevirapine. 1
Natural varianti777G → S Confers resistance to efavirenz and nevirapine. 1
Natural varianti777G → T Confers resistance to efavirenz, HBY 097 and nevirapine. 1
Natural varianti777G → V Confers resistance to efavirenz and nevirapine. 1
Natural varianti795H → Y Confers resistance to lamivudine, pyrophosphate analog PFA and zidovudine. 1
Natural varianti797L → W Confers resistance to zidovudine. 1
Natural varianti798R → K Confers resistance to lamivudine and zidovudine. 1
Natural varianti801L → F Confers resistance to ph-AZT and zidovudine. 1
Natural varianti802T → F Confers resistance to zidovudine; when associated with other amino acid changes. 1
Natural varianti802T → Y Confers resistance to zidovudine; when associated with other amino acid changes. 1
Natural varianti806K → E Confers resistance to zidovudine. 1
Natural varianti806K → Q Confers resistance to zidovudine; when associated with other amino acid changes. 1
Natural varianti806K → R Confers resistance to lamivudine, stavudine, zalcicabine and zidovudine. 1
Natural varianti812P → H Confers resistance to efavirenz, emivirine, HBY 097 and quinoxaline; when associated with A-17. 1
Natural varianti823P → L Confers resistance to atevirdine and delavirdine. 1
Natural varianti825K → T Confers resistance to atevirdine and zidovudine; when associated with other amino acid changes. 1
Natural varianti870L → I Confers resistance to delavirdine, efavirenz and nevirapine. 1
Natural varianti905Y → F Confers resistance to delavirdine and nevirapine. 1
Natural varianti920G → D Confers resistance to abacavir, lamivudine and zidovudine. 1
Natural varianti920G → E Confers resistance to abacavir, lamivudine and zidovudine. 1
Natural varianti973T → I Confers resistance to abacavir, lamivudine and zidovudine. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03455 Genomic RNA. Translation: AAB50259.1. Sequence problems.
AF033819 Genomic RNA. Translation: AAC82598.2. Sequence problems.
RefSeqiNP_057849.4. NC_001802.1.

Genome annotation databases

GeneIDi155348.
KEGGivg:155348.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Web resourcesi

HIV drug resistance mutations
hivdb

HIV drug resistance database

BioAfrica HIV proteomics resource

Pol entry

BioAfrica HIV proteomics resource

RT (p51) entry

BioAfrica HIV proteomics resource

RNase H (p15) entry

BioAfrica HIV proteomics resource

PR (p15) entry

BioAfrica HIV proteomics resource

IN (p31) entry

BioAfrica: HIV bioinformatics in Africa

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03455 Genomic RNA. Translation: AAB50259.1. Sequence problems.
AF033819 Genomic RNA. Translation: AAC82598.2. Sequence problems.
RefSeqiNP_057849.4. NC_001802.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A30X-ray2.00A/B489-587[»]
1BV7X-ray2.00A/B489-587[»]
1BV9X-ray2.00A/B489-587[»]
1BVENMR-A/B489-587[»]
1BVGNMR-A/B489-587[»]
1BWAX-ray1.90A/B489-587[»]
1BWBX-ray1.80A/B489-587[»]
1C0TX-ray2.70A588-1147[»]
B588-1027[»]
1C0UX-ray2.52A588-1147[»]
B588-1027[»]
1C1BX-ray2.50A588-1147[»]
B588-1428[»]
1C1CX-ray2.50A588-1147[»]
B588-1027[»]
1DMPX-ray2.00A/B489-587[»]
1DTQX-ray2.80A588-1147[»]
B588-1027[»]
1DTTX-ray3.00A588-1147[»]
B588-1027[»]
1E6JX-ray3.00P143-352[»]
1EP4X-ray2.50A588-1147[»]
B588-1027[»]
1ESKNMR-A390-430[»]
1EX4X-ray2.80A/B1199-1435[»]
1EXQX-ray1.60A/B1203-1356[»]
1FB7X-ray2.60A489-587[»]
1FK9X-ray2.50A588-1130[»]
B588-1027[»]
1FKOX-ray2.90A588-1130[»]
B588-1027[»]
1FKPX-ray2.90A588-1130[»]
B588-1027[»]
1G6LX-ray1.90A484-587[»]
1HIVX-ray2.00A/B489-587[»]
1HVHX-ray1.80A/B489-587[»]
1HVRX-ray1.80A/B489-587[»]
1HWRX-ray1.80A/B489-587[»]
1HXBX-ray2.30A/B489-587[»]
1JKHX-ray2.50A588-1147[»]
B588-1027[»]
1JLAX-ray2.50A588-1147[»]
B588-1027[»]
1JLBX-ray3.00A588-1147[»]
B588-1027[»]
1JLCX-ray3.00A588-1147[»]
B588-1027[»]
1JLEX-ray2.80A588-1147[»]
B588-1027[»]
1JLFX-ray2.60A588-1147[»]
B588-1027[»]
1JLGX-ray2.60A588-1147[»]
B588-1027[»]
1JLQX-ray3.00A588-1147[»]
B588-1027[»]
1KLMX-ray2.65A588-1147[»]
B588-1027[»]
1LV1X-ray2.10A484-587[»]
1LW0X-ray2.80A588-1147[»]
B588-1027[»]
1LW2X-ray3.00A588-1147[»]
B588-1027[»]
1LWCX-ray2.62A588-1147[»]
B588-1027[»]
1LWEX-ray2.81A588-1147[»]
B588-1027[»]
1LWFX-ray2.80A588-1147[»]
B588-1027[»]
1NCPNMR-N390-406[»]
1O1WNMR-A1014-1147[»]
1ODWX-ray2.10A/B489-587[»]
1ODYX-ray2.00A/B489-587[»]
1QBRX-ray1.80A/B489-587[»]
1QBSX-ray1.80A/B489-587[»]
1QBTX-ray2.10A/B489-587[»]
1QBUX-ray1.80A/B489-587[»]
1REVX-ray2.60A588-1147[»]
B588-1027[»]
1RT1X-ray2.55A588-1147[»]
B588-1027[»]
1RT2X-ray2.55A588-1147[»]
B588-1027[»]
1RT3X-ray3.00A588-1147[»]
B588-1027[»]
1RT4X-ray2.90A588-1147[»]
B588-1027[»]
1RT5X-ray2.90A588-1147[»]
B588-1027[»]
1RT6X-ray2.80A588-1147[»]
B588-1027[»]
1RT7X-ray3.00A588-1147[»]
B588-1027[»]
1RTDX-ray3.20B/D588-1027[»]
1RTHX-ray2.20A588-1147[»]
B588-1027[»]
1RTIX-ray3.00A588-1147[»]
B588-1027[»]
1RTJX-ray2.35A588-1147[»]
B588-1027[»]
1S1TX-ray2.40A588-1147[»]
B588-1027[»]
1S1UX-ray3.00A588-1147[»]
B588-1027[»]
1S1VX-ray2.60A588-1147[»]
B588-1027[»]
1S1WX-ray2.70A588-1147[»]
B588-1027[»]
1S1XX-ray2.80A588-1147[»]
B588-1027[»]
1T05X-ray3.00B588-1016[»]
1TAMNMR-A1-132[»]
1TKTX-ray2.60A588-1147[»]
B588-1027[»]
1TKXX-ray2.85A588-1147[»]
B588-1027[»]
1TKZX-ray2.81A588-1147[»]
B588-1027[»]
1TL1X-ray2.90A588-1147[»]
B588-1027[»]
1TL3X-ray2.80A588-1147[»]
B588-1027[»]
1VRTX-ray2.20A588-1147[»]
B588-1027[»]
1VRUX-ray2.40A588-1147[»]
B588-1027[»]
2HNDX-ray2.50A591-1124[»]
2HNYX-ray2.50A591-1124[»]
2HNZX-ray3.00A591-1124[»]
B594-1015[»]
2KODNMR-A/B276-363[»]
2NPHX-ray1.65A/B489-587[»]
2OPPX-ray2.55A591-1132[»]
B592-1018[»]
2OPQX-ray2.80A591-1124[»]
B592-1015[»]
2OPRX-ray2.90A589-1135[»]
B593-1018[»]
2OPSX-ray2.30A589-1130[»]
B593-1027[»]
2RF2X-ray2.40A588-1147[»]
B588-1027[»]
2RKIX-ray2.30A588-1147[»]
B588-1027[»]
2WHHX-ray1.69A489-587[»]
2WOMX-ray3.20A588-1147[»]
B588-1027[»]
2WONX-ray2.80A588-1147[»]
B588-1027[»]
2YNFX-ray2.36A588-1147[»]
B588-1015[»]
2YNGX-ray2.12A588-1147[»]
B588-1015[»]
2YNHX-ray2.90A588-1147[»]
B588-1015[»]
2YNIX-ray2.49A588-1147[»]
B588-1015[»]
3AO2X-ray1.80A/B1197-1359[»]
3C6TX-ray2.70A588-1147[»]
B588-1027[»]
3C6UX-ray2.70A588-1147[»]
B588-1027[»]
3DI6X-ray2.65A588-1148[»]
B588-1027[»]
3DLEX-ray2.50A588-1147[»]
B588-1027[»]
3DLGX-ray2.20A588-1147[»]
B588-1027[»]
3DM2X-ray3.10A588-1147[»]
B588-1027[»]
3DMJX-ray2.60A588-1147[»]
B588-1027[»]
3DOKX-ray2.90A588-1147[»]
B588-1027[»]
3DOLX-ray2.50A588-1147[»]
B588-1027[»]
3DOXX-ray2.00A484-587[»]
3DRPX-ray2.60A588-1147[»]
B588-1027[»]
3DRRX-ray2.89A588-1147[»]
B588-1027[»]
3DRSX-ray3.15A588-1147[»]
B588-1027[»]
3DYAX-ray2.30A588-1148[»]
B588-1027[»]
3E01X-ray2.95A588-1148[»]
B588-1027[»]
3FFIX-ray2.60A588-1147[»]
B588-1027[»]
3I0RX-ray2.98A588-1147[»]
B588-1027[»]
3I0SX-ray2.70A588-1147[»]
B588-1027[»]
3KJVX-ray3.10A588-1147[»]
B588-1027[»]
3KK1X-ray2.70A588-1147[»]
B588-1027[»]
3KK2X-ray2.90A588-1147[»]
B588-1027[»]
3KK3X-ray2.90A588-1147[»]
B588-1027[»]
3KT2X-ray1.65A484-587[»]
3KT5X-ray1.80A484-587[»]
3LAKX-ray2.30A/B588-1147[»]
3LALX-ray2.51A/B588-1147[»]
3LAMX-ray2.76A/B588-1147[»]
3LANX-ray2.55A/B588-1147[»]
3LP0<