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P07953

- F261_RAT

UniProt

P07953 - F261_RAT

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Protein

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

Gene

Pfkfb1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Synthesis and degradation of fructose 2,6-bisphosphate.

Catalytic activityi

Beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate.

Enzyme regulationi

Phosphorylation at Ser-33 inhibits the kinase and activates the bisphosphatase.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei82 – 821Fructose 6-phosphateBy similarity
Binding sitei105 – 1051Fructose 6-phosphateBy similarity
Active sitei131 – 1311Sequence Analysis
Binding sitei133 – 1331Fructose 6-phosphateBy similarity
Binding sitei139 – 1391Fructose 6-phosphateBy similarity
Active sitei161 – 1611Sequence Analysis
Binding sitei175 – 1751Fructose 6-phosphateBy similarity
Binding sitei196 – 1961Fructose 6-phosphateBy similarity
Binding sitei200 – 2001Fructose 6-phosphateBy similarity
Binding sitei258 – 2581Fructose 2,6-bisphosphateBy similarity
Active sitei259 – 2591Tele-phosphohistidine intermediate1 Publication
Binding sitei265 – 2651Fructose 2,6-bisphosphateBy similarity
Binding sitei271 – 2711Fructose 2,6-bisphosphate; via amide nitrogen
Binding sitei308 – 3081Fructose 2,6-bisphosphateBy similarity
Active sitei328 – 3281Proton donor/acceptor1 Publication
Binding sitei339 – 3391Fructose 2,6-bisphosphate
Binding sitei353 – 3531Fructose 2,6-bisphosphate
Binding sitei357 – 3571Fructose 2,6-bisphosphate
Binding sitei368 – 3681Fructose 2,6-bisphosphate
Active sitei393 – 3931Proton donor/acceptor1 Publication
Binding sitei394 – 3941Fructose 2,6-bisphosphate
Binding sitei398 – 3981Fructose 2,6-bisphosphate
Binding sitei430 – 4301ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi49 – 579ATPBy similarity
Nucleotide bindingi170 – 1756ATPBy similarity
Nucleotide bindingi350 – 3534ATP
Nucleotide bindingi394 – 3985ATP

GO - Molecular functioni

  1. 6-phosphofructo-2-kinase activity Source: RGD
  2. ATP binding Source: RGD
  3. fructose-2,6-bisphosphate 2-phosphatase activity Source: UniProtKB
  4. fructose-6-phosphate binding Source: RGD
  5. identical protein binding Source: IntAct
  6. kinase binding Source: RGD

GO - Biological processi

  1. carbohydrate phosphorylation Source: RGD
  2. dephosphorylation Source: GOC
  3. fructose 2,6-bisphosphate metabolic process Source: UniProtKB
  4. fructose metabolic process Source: InterPro
  5. organ regeneration Source: RGD
  6. positive regulation of glucokinase activity Source: RGD
  7. response to cAMP Source: RGD
  8. response to glucagon Source: RGD
  9. response to glucocorticoid Source: RGD
  10. response to insulin Source: RGD
  11. response to starvation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.1.3.46. 5301.
ReactomeiREACT_217998. Gluconeogenesis.
REACT_225694. Glycolysis.
SABIO-RKP07953.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1
Short name:
6PF-2-K/Fru-2,6-P2ase 1
Short name:
PFK/FBPase 1
Alternative name(s):
6PF-2-K/Fru-2,6-P2ase liver isozyme
Including the following 2 domains:
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
Gene namesi
Name:Pfkfb1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome X

Organism-specific databases

RGDi3307. Pfkfb1.

Subcellular locationi

GO - Cellular componenti

  1. 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex Source: UniProtKB
  2. cytosol Source: Reactome
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 4714706-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1PRO_0000179962Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei33 – 331Phosphoserine; by PKA1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP07953.

PTM databases

PhosphoSiteiP07953.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

ExpressionAtlasiP07953. baseline and differential.
GenevestigatoriP07953.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-709873,EBI-709873

Protein-protein interaction databases

IntActiP07953. 2 interactions.
MINTiMINT-8147404.

Structurei

Secondary structure

1
471
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi253 – 2586
Helixi263 – 2675
Helixi278 – 29215
Beta strandi300 – 3067
Helixi307 – 3148
Turni315 – 3173
Beta strandi321 – 3233
Helixi324 – 3263
Helixi332 – 3343
Helixi339 – 3457
Helixi347 – 3559
Turni357 – 3593
Helixi368 – 3747
Helixi376 – 3838
Beta strandi386 – 3927
Helixi394 – 40411
Turni409 – 4113
Helixi412 – 4143
Beta strandi421 – 4288
Beta strandi431 – 4388

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C7ZX-ray2.60A/B252-441[»]
1C80X-ray2.20A/B252-441[»]
1C81X-ray2.50A252-441[»]
1FBTX-ray2.00A/B252-441[»]
1TIPX-ray2.20A/B252-441[»]
ProteinModelPortaliP07953.
SMRiP07953. Positions 7-471.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07953.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2502496-phosphofructo-2-kinaseAdd
BLAST
Regioni251 – 471221Fructose-2,6-bisphosphataseAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the phosphoglycerate mutase family.Curated

Phylogenomic databases

eggNOGiCOG0406.
GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP07953.
KOiK01103.
OMAiNIRGRIG.
OrthoDBiEOG7M3J03.
PhylomeDBiP07953.
TreeFamiTF313541.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR016260. Bifunct_6PFK/fruc_bisP_Ptase.
IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR027417. P-loop_NTPase.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view]
PANTHERiPTHR10606. PTHR10606. 1 hit.
PfamiPF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000709. 6PFK_2-Ptase. 1 hit.
PRINTSiPR00991. 6PFRUCTKNASE.
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEiPS00175. PG_MUTASE. 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 alternative splicing. Align

Isoform 1 (identifier: P07953-1) [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
MSREMGELTQ TRLQKIWIPH SSSSSVLQRR RGSSIPQFTN SPTMVIMVGL
60 70 80 90 100
PARGKTYIST KLTRYLNWIG TPTKVFNLGQ YRREAVSYRN YEFFRPDNTE
110 120 130 140 150
AQLIRKQCAL AALKDVHKYL SREEGHVAVF DATNTTRERR SLILQFAKEH
160 170 180 190 200
GYKVFFIESI CNDPEIIAEN IKQVKLGSPD YIDCDQEKVL EDFLKRIECY
210 220 230 240 250
EINYQPLDEE LDSHLSYIKI FDVGTRYMVN RVQDHVQSRT AYYLMNIHVT
260 270 280 290 300
PRSIYLCRHG ESELNLRGRI GGDSGLSARG KQYAYALANF IRSQGISSLK
310 320 330 340 350
VWTSHMKRTI QTAEALGVPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF
360 370 380 390 400
ALRDQDKYRY RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL
410 420 430 440 450
LAYFLDKSSD ELPYLKCPLH TVLKLTPVAY GCRVESIYLN VEAVNTHRDK
460 470
PENVDITREA EEALDTVPAH Y
Length:471
Mass (Da):54,763
Last modified:January 23, 2007 - v3
Checksum:iE307AF13945E0FCD
GO
Isoform 2 (identifier: P07953-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MSREMGELTQTRLQKIWIPHSSSSSVLQRRRGS → MEEKASKRTA

Show »
Length:448
Mass (Da):52,070
Checksum:i3DCD00D54929917D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351T → Y(PubMed:2547611)Curated
Sequence conflicti135 – 1351T → Y(PubMed:2848802)Curated
Sequence conflicti135 – 1351T → Y(PubMed:2826464)Curated
Sequence conflicti138 – 1381E → F(PubMed:2547611)Curated
Sequence conflicti257 – 2571Missing AA sequence (PubMed:3040762)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333MSREM…RRRGS → MEEKASKRTA in isoform 2. 1 PublicationVSP_004674Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00702 mRNA. Translation: CAA68694.1.
X15579 mRNA. Translation: CAA33606.1.
X15580 mRNA. Translation: CAA33607.1.
M26215 Genomic DNA. Translation: AAA02888.2.
M26216 Genomic DNA. Translation: AAA02889.1.
J04197 mRNA. Translation: AAA79008.1.
M27886 Genomic DNA. Translation: AAA58780.1.
PIRiS11761. KIRTFB.
RefSeqiNP_036753.4. NM_012621.4. [P07953-1]
UniGeneiRn.10115.

Genome annotation databases

EnsembliENSRNOT00000000178; ENSRNOP00000000178; ENSRNOG00000000165. [P07953-2]
ENSRNOT00000033656; ENSRNOP00000035212; ENSRNOG00000000165. [P07953-1]
GeneIDi24638.
KEGGirno:24638.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00702 mRNA. Translation: CAA68694.1 .
X15579 mRNA. Translation: CAA33606.1 .
X15580 mRNA. Translation: CAA33607.1 .
M26215 Genomic DNA. Translation: AAA02888.2 .
M26216 Genomic DNA. Translation: AAA02889.1 .
J04197 mRNA. Translation: AAA79008.1 .
M27886 Genomic DNA. Translation: AAA58780.1 .
PIRi S11761. KIRTFB.
RefSeqi NP_036753.4. NM_012621.4. [P07953-1 ]
UniGenei Rn.10115.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C7Z X-ray 2.60 A/B 252-441 [» ]
1C80 X-ray 2.20 A/B 252-441 [» ]
1C81 X-ray 2.50 A 252-441 [» ]
1FBT X-ray 2.00 A/B 252-441 [» ]
1TIP X-ray 2.20 A/B 252-441 [» ]
ProteinModelPortali P07953.
SMRi P07953. Positions 7-471.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P07953. 2 interactions.
MINTi MINT-8147404.

PTM databases

PhosphoSitei P07953.

Proteomic databases

PRIDEi P07953.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000000178 ; ENSRNOP00000000178 ; ENSRNOG00000000165 . [P07953-2 ]
ENSRNOT00000033656 ; ENSRNOP00000035212 ; ENSRNOG00000000165 . [P07953-1 ]
GeneIDi 24638.
KEGGi rno:24638.

Organism-specific databases

CTDi 5207.
RGDi 3307. Pfkfb1.

Phylogenomic databases

eggNOGi COG0406.
GeneTreei ENSGT00390000018751.
HOGENOMi HOG000181112.
HOVERGENi HBG005628.
InParanoidi P07953.
KOi K01103.
OMAi NIRGRIG.
OrthoDBi EOG7M3J03.
PhylomeDBi P07953.
TreeFami TF313541.

Enzyme and pathway databases

BRENDAi 3.1.3.46. 5301.
Reactomei REACT_217998. Gluconeogenesis.
REACT_225694. Glycolysis.
SABIO-RK P07953.

Miscellaneous databases

EvolutionaryTracei P07953.
NextBioi 603924.
PROi P07953.

Gene expression databases

ExpressionAtlasi P07953. baseline and differential.
Genevestigatori P07953.

Family and domain databases

Gene3Di 3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProi IPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR016260. Bifunct_6PFK/fruc_bisP_Ptase.
IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR027417. P-loop_NTPase.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view ]
PANTHERi PTHR10606. PTHR10606. 1 hit.
Pfami PF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000709. 6PFK_2-Ptase. 1 hit.
PRINTSi PR00991. 6PFRUCTKNASE.
SMARTi SM00855. PGAM. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEi PS00175. PG_MUTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete nucleotide sequence coding for rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase derived from a cDNA clone."
    Darville M.I., Crepin K.M., Vandekerckhove J., van Damme J., Octave J.-N., Rider M.H., Marchand M.J., Hue L., Rousseau G.G.
    FEBS Lett. 224:317-321(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1), PROTEIN SEQUENCE OF 16-29; 65-74; 90-105; 123-137; 189-195; 240-252; 259-266 AND 309-324 (ISOFORM 1).
    Strain: Wistar.
    Tissue: Liver.
  2. "Isolation of a cDNA clone for rat liver 6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase."
    Colosa A.D., Lively M.O., El-Maghrabi M.R., Pilkis S.J.
    Biochem. Biophys. Res. Commun. 143:1092-1098(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
    Strain: Sprague-Dawley.
  3. "Characterization of distinct mRNAs coding for putative isozymes of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
    Crepin K.M., Darville M.I., Hue L., Rousseau G.G.
    Eur. J. Biochem. 183:433-440(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Strain: Wistar.
    Tissue: Liver.
  4. "Induction of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase mRNA by refeeding and insulin."
    Colosia A.D., Marker A.J., Lange A.J., El-Maghrabi M.R., Granner D.K., Tauler A., Pilkis J., Pilkis S.J.
    J. Biol. Chem. 263:18669-18677(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  5. "Complete amino acid sequence of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
    Lively M.O., El-Maghrabi M.R., Pilkis J., D'Angelo G., Colosia A.D., Ciavola J.A., Fraser B.A., Pilkis S.J.
    J. Biol. Chem. 263:839-849(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (ISOFORM 1), ACETYLATION AT SER-2.
    Tissue: Liver.
  6. "Cloning and expression in Escherichia coli of a rat hepatoma cell cDNA coding for 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
    Crepin K.M., Darville M.I., Michel A., Hue L., Rousseau G.G.
    Biochem. J. 264:151-160(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2).
    Strain: Wistar.
    Tissue: Liver.
  7. "Active site sequence of hepatic fructose-2,6-bisphosphatase. Homology in primary structure with phosphoglycerate mutase."
    Pilkis S.J., Lively M.O., El-Maghrabi M.R.
    J. Biol. Chem. 262:12672-12675(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 220-267.
    Tissue: Liver.
  8. "5' flanking sequence and structure of a gene encoding rat 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
    Darville M.I., Crepin K.M., Hue L., Rousseau G.G.
    Proc. Natl. Acad. Sci. U.S.A. 86:6543-6547(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32 (ISOFORM 1), PROTEIN SEQUENCE OF 2-10 (ISOFORM 2).
  9. "Catalytic site of rat liver and bovine heart fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase. Identification of fructose 6-phosphate binding site."
    Kitamura K., Uyeda K., Hartman F.C., Kangawa K., Matsuo H.
    J. Biol. Chem. 264:6344-6348(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 106-114, REGION.
  10. "Evolution of a bifunctional enzyme: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
    Bazan J.F., Fletterick R.J., Pilkis S.J.
    Proc. Natl. Acad. Sci. U.S.A. 86:9642-9646(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS.
  11. "Covalent control of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: insights into autoregulation of a bifunctional enzyme."
    Kurland I.J., Pilkis S.J.
    Protein Sci. 4:1023-1037(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-33, ENZYME REGULATION.
  12. "Crystal structure of the rat liver fructose-2,6-bisphosphatase based on selenomethionine multiwavelength anomalous dispersion phases."
    Lee Y.-H., Ogata C., Pflugrath J.W., Levitt D.G., Sarma R., Banaszak L.J., Pilkis S.J.
    Biochemistry 35:6010-6019(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    Tissue: Liver.
  13. "Crystal structure of a trapped phosphoenzyme during a catalytic reaction."
    Lee Y.-H., Olson T.W., Ogata C.M., Levitt D.G., Banaszak L.J., Lange A.J.
    Nat. Struct. Biol. 4:615-618(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 251-441 IN COMPLEX WITH FRUCTOSE 6-PHOSPHATE, ACTIVE SITE.
  14. "Reaction mechanism of fructose-2,6-bisphosphatase suggested by the crystal structures of a pseudo-Michaelis complex and metabolite complexes."
    Lee Y.-H., Olson T.W., McClard R.W., Witte J.F., McFarlan S.C., Banaszak L.J., Levitt D.G., Lange A.J.
    Submitted (APR-2000) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 252-440 IN COMPLEXES WITH SUBSTRATE ANALOG AND WITH GTP.

Entry informationi

Entry nameiF261_RAT
AccessioniPrimary (citable) accession number: P07953
Secondary accession number(s): P16119
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3