Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q0ED31

- Q0ED31_9HIV1

UniProt

Q0ED31 - Q0ED31_9HIV1

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Envelope glycoprotein gp160

Gene

env

Organism
Human immunodeficiency virus 1
Status
Unreviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

The envelope glyprotein gp160 precursor down-modulates cell surface CD4 antigen by interacting with it in the endoplasmic reticulum and blocking its transport to the cell surface.UniRule annotationSAAS annotation
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves.SAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei61 – 611MannoseCombined sources

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. evasion or tolerance by virus of host immune response Source: UniProtKB-KW
  3. membrane fusion involved in viral entry into host cell Source: UniProtKB-KW
  4. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

ApoptosisSAAS annotation, Fusion of virus membrane with host membraneSAAS annotation, Host-virus interaction, Viral attachment to host cellUniRule annotationSAAS annotation, Viral immunoevasionUniRule annotation, Viral penetration into host cytoplasm, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein gp160UniRule annotationSAAS annotation
Gene namesi
Name:envImported
OrganismiHuman immunodeficiency virus 1Imported
Taxonomic identifieri11676 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

Virion membrane SAAS annotation; Single-pass type I membrane protein SAAS annotation. Host cell membrane SAAS annotation; Single-pass type I membrane protein SAAS annotation. Host endosome membrane SAAS annotation; Single-pass type I membrane protein SAAS annotation

GO - Cellular componenti

  1. host cell endosome membrane Source: UniProtKB-SubCell
  2. host cell plasma membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. viral envelope Source: UniProtKB-KW
  5. virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cell membraneSAAS annotation, Host endosomeSAAS annotation, Host membrane, Membrane, Viral envelope proteinUniRule annotationSAAS annotation, Virion

Pathology & Biotechi

Keywords - Diseasei

AIDSUniRule annotation

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi53 ↔ 73Combined sources
Glycosylationi87 – 871N-linked (GlcNAc...)Combined sources
Disulfide bondi118 ↔ 207Combined sources
Glycosylationi160 – 1601N-linked (GlcNAc...)Combined sources
Glycosylationi188 – 1881N-linked (GlcNAc...)Combined sources
Disulfide bondi220 ↔ 249Combined sources
Disulfide bondi230 ↔ 241Combined sources
Glycosylationi236 – 2361N-linked (GlcNAc...)Combined sources
Disulfide bondi238 ↔ 439Combined sources
Glycosylationi243 – 2431N-linked (GlcNAc...)Combined sources
Glycosylationi264 – 2641N-linked (GlcNAc...)Combined sources
Glycosylationi278 – 2781N-linked (GlcNAc...)Combined sources
Glycosylationi291 – 2911N-linked (GlcNAc...)Combined sources
Disulfide bondi297 ↔ 332Combined sources
Glycosylationi297 – 2971N-linked (GlcNAc...)Combined sources
Disulfide bondi332 ↔ 412Combined sources
Disulfide bondi332 ↔ 385Combined sources
Glycosylationi335 – 3351N-linked (GlcNAc...)Combined sources
Glycosylationi356 – 3561N-linked (GlcNAc...)Combined sources
Glycosylationi386 – 3861N-linked (GlcNAc...)Combined sources
Glycosylationi392 – 3921N-linked (GlcNAc...)Combined sources
Disulfide bondi395 ↔ 404Combined sources
Glycosylationi442 – 4421N-linked (GlcNAc...)Combined sources

Keywords - PTMi

Cleavage on pair of basic residuesUniRule annotation, Disulfide bondSAAS annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NGBX-ray2.68A/D/G/I43-122[»]
A/D/G/I201-303[»]
A/D/G/I325-486[»]
3SE8X-ray1.90G43-486[»]
3SE9X-ray2.00G43-486[»]
3TGTX-ray1.90A43-486[»]
3U7YX-ray2.45G43-122[»]
G201-303[»]
G325-486[»]
4DKOX-ray1.98A/C43-486[»]
4DKPX-ray1.80A/C43-486[»]
4DKQX-ray1.89A43-486[»]
4DKRX-ray1.80A/C43-486[»]
4DKUX-ray2.49A/B43-122[»]
A/B201-303[»]
A/B325-486[»]
4DKVX-ray2.18A/B43-122[»]
A/B201-303[»]
A/B325-486[»]
4DVSX-ray2.10A/B43-122[»]
A/B201-302[»]
A/B325-486[»]
4DVTX-ray2.40A/B88-122[»]
A/B201-341[»]
A/B457-486[»]
4DVVX-ray1.94A/B43-122[»]
A/B201-303[»]
A/B325-486[»]
4DVWX-ray2.20A/B43-122[»]
A/B201-303[»]
A/B325-486[»]
4DVXX-ray2.40A/B43-122[»]
A/B201-303[»]
A/B325-486[»]
4H8WX-ray1.85G43-486[»]
4I54X-ray2.50A/B43-486[»]
4JB9X-ray2.60G43-486[»]
4JDTX-ray3.26G43-486[»]
4JKPX-ray2.82G43-486[»]
4JPVX-ray2.83G43-486[»]
4JPWX-ray2.90G43-486[»]
4LSPX-ray2.15G43-486[»]
4LSQX-ray2.25G43-486[»]
4LSRX-ray2.28G43-486[»]
4LSUX-ray2.30G43-486[»]
4OLUX-ray2.20G43-122[»]
G201-303[»]
G325-486[»]
4OLVX-ray2.50G43-122[»]
G201-303[»]
G325-486[»]
4OLWX-ray2.71G43-122[»]
G201-303[»]
G325-486[»]
4OLXX-ray2.20G43-122[»]
G201-303[»]
G325-486[»]
4OLYX-ray2.35G43-122[»]
G201-303[»]
G325-486[»]
4OLZX-ray2.10G43-122[»]
G201-303[»]
G325-486[»]
4OM0X-ray2.29G43-122[»]
G201-303[»]
G325-486[»]
4OM1X-ray2.13G43-122[»]
G201-303[»]
G325-486[»]
4P9HX-ray3.00G43-122[»]
G201-303[»]
G325-486[»]
SMRiQ0ED31. Positions 82-486, 499-584.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ0ED31.

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helixSAAS annotation

Family and domain databases

Gene3Di2.170.40.20. 2 hits.
InterProiIPR000777. HIV1_GP160.
IPR000328. Retroviral_envelope_protein.
[Graphical view]
PfamiPF00516. GP120. 1 hit.
PF00517. GP41. 1 hit.
[Graphical view]
SUPFAMiSSF56502. SSF56502. 2 hits.

Sequencei

Sequence statusi: Complete.

Q0ED31-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRVKETQMNW PNLWKWGTLI LGLVIICSAS DNLWVTVYYG VPVWKDADTT
60 70 80 90 100
LFCASDAKAH ETEVHNVWAT HACVPTDPNP QEIHLENVTE NFNMWKNNMV
110 120 130 140 150
EQMQEDVISL WDQSLQPCVK LTPLCVTLHC TTAKLTNVTN ITNVPNIGNI
160 170 180 190 200
TDEVRNCSFN MTTEIRDKKQ KVHALFYKLD IVQIEDKNDS SKYRLINCNT
210 220 230 240 250
SVIKQACPKI SFDPIPIHYC TPAGYVILKC NDKNFNGTGP CKNVSSVQCT
260 270 280 290 300
HGIKPVVSTQ LLLNGSLAEE EIIIRSENLT NNAKTIIVHL NKSVEINCTR
310 320 330 340 350
PSNNMRTSMR IGPGQVFYRT GSITGDIRKA YCEINGTKWN KVLKQVTEKL
360 370 380 390 400
KEHFNNKTII FQPPSGGDLE ITMHHFNCRG EFFYCNTTQL FNNTCIGNET
410 420 430 440 450
MKGCNGTITL PCKIKQIINM WQGTGQAMYA PPIDGKINCV SNITGILLTR
460 470 480 490 500
DGGANNTSNE TFRPGGGNIK DNWRSELYKY KVVQIEPLGI APTRAKRRVV
510 520 530 540 550
EREKRAVGIG AMIFGFLGAA GSTMGAASIT LTVQARQLLS GIVQQQSNLL
560 570 580 590 600
RAIEAQQHLL QLTVWGIKQL QARVLAVERY LKDQKFLGLW GCSGKIICTT
610 620 630 640 650
AVPWNSTWSN KSFEEIWNNM TWIEWEREIS NYTNQIYEIL TESQNQQDRN
660 670 680 690 700
EKDLLELDKW ASLWNWFDIT NWLWYIKIFI MIVGGLIGLR IIFAVLSIVN
710 720 730 740 750
RVRQGYSPLS FQTPIHHQRE PDRPERIEEG GGEQGRDRSV RLVSGFLSLA
760 770 780 790 800
WDDLRSLCLF SYHRLRDFIL IATRTVELLG HSSLKGLRRG WEGLKYLGNL
810 820 830 840 850
LLYWGQELKI SAISLLNTTA IAVAGWTDRV IEVAQGAWRA ILHIPRRIRQ

GLERTLL
Length:857
Mass (Da):97,310
Last modified:October 17, 2006 - v1
Checksum:iAA83C4FF189CCD0E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB253424 Genomic DNA. Translation: BAF31367.1.
AB253425 Genomic DNA. Translation: BAF31376.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB253424 Genomic DNA. Translation: BAF31367.1 .
AB253425 Genomic DNA. Translation: BAF31376.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3NGB X-ray 2.68 A/D/G/I 43-122 [» ]
A/D/G/I 201-303 [» ]
A/D/G/I 325-486 [» ]
3SE8 X-ray 1.90 G 43-486 [» ]
3SE9 X-ray 2.00 G 43-486 [» ]
3TGT X-ray 1.90 A 43-486 [» ]
3U7Y X-ray 2.45 G 43-122 [» ]
G 201-303 [» ]
G 325-486 [» ]
4DKO X-ray 1.98 A/C 43-486 [» ]
4DKP X-ray 1.80 A/C 43-486 [» ]
4DKQ X-ray 1.89 A 43-486 [» ]
4DKR X-ray 1.80 A/C 43-486 [» ]
4DKU X-ray 2.49 A/B 43-122 [» ]
A/B 201-303 [» ]
A/B 325-486 [» ]
4DKV X-ray 2.18 A/B 43-122 [» ]
A/B 201-303 [» ]
A/B 325-486 [» ]
4DVS X-ray 2.10 A/B 43-122 [» ]
A/B 201-302 [» ]
A/B 325-486 [» ]
4DVT X-ray 2.40 A/B 88-122 [» ]
A/B 201-341 [» ]
A/B 457-486 [» ]
4DVV X-ray 1.94 A/B 43-122 [» ]
A/B 201-303 [» ]
A/B 325-486 [» ]
4DVW X-ray 2.20 A/B 43-122 [» ]
A/B 201-303 [» ]
A/B 325-486 [» ]
4DVX X-ray 2.40 A/B 43-122 [» ]
A/B 201-303 [» ]
A/B 325-486 [» ]
4H8W X-ray 1.85 G 43-486 [» ]
4I54 X-ray 2.50 A/B 43-486 [» ]
4JB9 X-ray 2.60 G 43-486 [» ]
4JDT X-ray 3.26 G 43-486 [» ]
4JKP X-ray 2.82 G 43-486 [» ]
4JPV X-ray 2.83 G 43-486 [» ]
4JPW X-ray 2.90 G 43-486 [» ]
4LSP X-ray 2.15 G 43-486 [» ]
4LSQ X-ray 2.25 G 43-486 [» ]
4LSR X-ray 2.28 G 43-486 [» ]
4LSU X-ray 2.30 G 43-486 [» ]
4OLU X-ray 2.20 G 43-122 [» ]
G 201-303 [» ]
G 325-486 [» ]
4OLV X-ray 2.50 G 43-122 [» ]
G 201-303 [» ]
G 325-486 [» ]
4OLW X-ray 2.71 G 43-122 [» ]
G 201-303 [» ]
G 325-486 [» ]
4OLX X-ray 2.20 G 43-122 [» ]
G 201-303 [» ]
G 325-486 [» ]
4OLY X-ray 2.35 G 43-122 [» ]
G 201-303 [» ]
G 325-486 [» ]
4OLZ X-ray 2.10 G 43-122 [» ]
G 201-303 [» ]
G 325-486 [» ]
4OM0 X-ray 2.29 G 43-122 [» ]
G 201-303 [» ]
G 325-486 [» ]
4OM1 X-ray 2.13 G 43-122 [» ]
G 201-303 [» ]
G 325-486 [» ]
4P9H X-ray 3.00 G 43-122 [» ]
G 201-303 [» ]
G 325-486 [» ]
SMRi Q0ED31. Positions 82-486, 499-584.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q0ED31.

Family and domain databases

Gene3Di 2.170.40.20. 2 hits.
InterProi IPR000777. HIV1_GP160.
IPR000328. Retroviral_envelope_protein.
[Graphical view ]
Pfami PF00516. GP120. 1 hit.
PF00517. GP41. 1 hit.
[Graphical view ]
SUPFAMi SSF56502. SSF56502. 2 hits.
ProtoNeti Search...

Publicationsi

  1. "Construction and characterization of HIV-1 CRF01_AE infectious molecular clones."
    Sakamoto Y., Takekawa N., Tatsumi M.
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 93TH057Imported.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 43-122; 201-303 AND 325-486, ACTIVE SITE, GLYCOSYLATION AT ASN-87; ASN-236; ASN-243; ASN-264; ASN-278; ASN-291; ASN-297; ASN-335; ASN-386; ASN-392 AND ASN-442.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 43-486, ACTIVE SITE, GLYCOSYLATION AT ASN-87; ASN-160 AND ASN-188.
  4. "Increasing the potency and breadth of an HIV antibody by using structure-based rational design."
    Diskin R., Scheid J.F., Marcovecchio P.M., West A.P., Klein F., Gao H., Gnanapragasam P.N., Abadir A., Seaman M.S., Nussenzweig M.C., Bjorkman P.J.
    Science 334:1289-1293(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 43-122; 201-303 AND 325-486, ACTIVE SITE, GLYCOSYLATION AT ASN-87; ASN-236; ASN-264; ASN-291; ASN-297 AND ASN-386.
  5. "Structure-based design, synthesis, and characterization of dual hotspot small-molecule HIV-1 entry inhibitors."
    LaLonde J.M., Kwon Y.D., Jones D.M., Sun A.W., Courter J.R., Soeta T., Kobayashi T., Princiotto A.M., Wu X., Schon A., Freire E., Kwong P.D., Mascola J.R., Sodroski J., Madani N., Smith A.B.
    J. Med. Chem. 55:4382-4396(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 43-486, ACTIVE SITE, GLYCOSYLATION AT ASN-160 AND ASN-188.
  6. "Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops."
    Kwon Y.D., Finzi A., Wu X., Dogo-Isonagie C., Lee L.K., Moore L.R., Schmidt S.D., Stuckey J., Yang Y., Zhou T., Zhu J., Vicic D.A., Debnath A.K., Shapiro L., Bewley C.A., Mascola J.R., Sodroski J.G., Kwong P.D.
    Proc. Natl. Acad. Sci. U.S.A. 109:5663-5668(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 43-486, ACTIVE SITE, GLYCOSYLATION AT ASN-160 AND ASN-188.
  7. "Antiviral activity and binding mode of next generation CD4-mimetics."
    Curreli F., Kwon Y.D., Zhang H, Kwong P.D., Debnath A.K.
    Submitted (FEB-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 43-122; 201-303 AND 325-486, ACTIVE SITE, GLYCOSYLATION AT ASN-236; ASN-243; ASN-264; ASN-278; ASN-291; ASN-297; ASN-335; ASN-356; ASN-386 AND ASN-442.
  8. "Structure-Based Design and Synthesis of an HIV-1 Entry Inhibitor Exploiting X-Ray and Thermodynamic Characterization."
    Lalonde J.M., Le-Khac M., Jones D.M., Courter J.R., Park J., Schon A., Princiotto A.M., Wu X., Mascola J.R., Freire E., Sodroski J., Madani N., Hendrickson W.A., Smith A.B.
    ACS Med. Chem. Lett. 4:338-343(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 43-486, ACTIVE SITE, GLYCOSYLATION AT ASN-160 AND ASN-188.
  9. "Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization."
    Klein F., Diskin R., Scheid J.F., Gaebler C., Mouquet H., Georgiev I.S., Pancera M., Zhou T., Incesu R.B., Fu B.Z., Gnanapragasam P.N., Oliveira T.Y., Seaman M.S., Kwong P.D., Bjorkman P.J., Nussenzweig M.C.
    Cell 153:126-138(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.83 ANGSTROMS) OF 43-486, ACTIVE SITE, GLYCOSYLATION AT ASN-160 AND ASN-188.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 43-486, ACTIVE SITE, GLYCOSYLATION AT ASN-87; ASN-160 AND ASN-188.
  11. "Restricting HIV-1 pathways for escape using rationally designed anti-HIV-1 antibodies."
    Diskin R., Klein F., Horwitz J.A., Halper-Stromberg A., Sather D.N., Marcovecchio P.M., Lee T., West A.P., Gao H., Seaman M.S., Stamatatos L., Nussenzweig M.C., Bjorkman P.J.
    J. Exp. Med. 210:1235-1249(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF 43-486, ACTIVE SITE, GLYCOSYLATION AT ASN-160 AND ASN-188.
  12. "Structural basis for HIV-1 gp120 recognition by a germ-line version of a broadly neutralizing antibody."
    Scharf L., West A.P., Gao H., Lee T., Scheid J.F., Nussenzweig M.C., Bjorkman P.J., Diskin R.
    Proc. Natl. Acad. Sci. U.S.A. 110:6049-6054(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.26 ANGSTROMS) OF 43-486, ACTIVE SITE, GLYCOSYLATION AT ASN-188.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 43-486, ACTIVE SITE, GLYCOSYLATION AT ASN-160 AND ASN-188.
  14. "Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike."
    Scharf L., Scheid J.F., Lee J.H., West A.P., Chen C., Gao H., Gnanapragasam P.N., Mares R., Seaman M.S., Ward A.B., Nussenzweig M.C., Bjorkman P.J.
    Cell Rep. 7:785-795(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 43-122; 201-303 AND 325-486 IN COMPLEX WITH MANNOSE, ACTIVE SITE, GLYCOSYLATION AT ASN-236; ASN-243; ASN-264; ASN-278; ASN-297; ASN-356 AND ASN-386.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 43-122; 201-303 AND 325-486, ACTIVE SITE, GLYCOSYLATION AT ASN-236; ASN-243; ASN-264; ASN-278; ASN-291; ASN-297; ASN-335; ASN-386; ASN-392 AND ASN-442.
  16. "Structural Definition of an Antibody-Dependent Cellular Cytotoxicity Response Implicated in Reduced Risk for HIV-1 Infection."
    Acharya P., Tolbert W.D., Gohain N., Wu X., Yu L., Liu T., Huang W., Huang C.C., Kwon Y.D., Louder R.K., Luongo T.S., McLellan J.S., Pancera M., Yang Y., Zhang B., Flinko R., Foulke J.S., Sajadi M.M.
    , Kamin-Lewis R., Robinson J.E., Martin L., Kwong P.D., Guan Y., DeVico A.L., Lewis G.K., Pazgier M.
    J. Virol. 88:12895-12906(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 43-486, ACTIVE SITE, GLYCOSYLATION AT ASN-188.
  17. "Crystal structures of HIV-1 gp120 envelope glycoprotein in complex with NBD analogues that target the CD4-binding site."
    Kwon Y.D., LaLonde J.M., Yang Y., Elban M.A., Sugawara A., Courter J.R., Jones D.M., Smith A.B., Debnath A.K., Kwong P.D.
    PLoS ONE 9:e85940-e85940(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 43-122; 201-303 AND 325-486, ACTIVE SITE, GLYCOSYLATION AT ASN-236; ASN-243; ASN-264; ASN-278; ASN-291; ASN-297; ASN-335; ASN-356; ASN-386; ASN-392 AND ASN-442.

Entry informationi

Entry nameiQ0ED31_9HIV1
AccessioniPrimary (citable) accession number: Q0ED31
Entry historyi
Integrated into UniProtKB/TrEMBL: October 17, 2006
Last sequence update: October 17, 2006
Last modified: January 7, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.