Structure of PDB 2vpq Chain B

Receptor sequence
>2vpqB (length=448) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
KKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVG
PTLSKDSYLNIPNILSIATSTGCDGVHPGYGFLAENADFAELCEACQLKF
IGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIG
YPVIIKATAGGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKF
IENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEEAPSPILDDETR
REMGNAAVRAAKAVNYENAGTIEFIYDLNDNKFYFMEMNTRIQVEHPVTE
MVTGIDLVKLQLQVAMGDVLPYKQEDIKLTGHAIEFRINAENPYKNFMPS
PGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAIM
AGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQNSIMND
3D structure
PDB2vpq Structural Evidence for Substrate-Induced Synergism and Half-Sites Reactivity in Biotin Carboxylase.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) V117 K157 H207 R233 T272 E274 E288 N290 R292 E296 R338
Catalytic site (residue number reindexed from 1) V116 K156 H206 R232 T271 E273 E287 N289 R291 E295 R337
Enzyme Commision number 6.3.4.14: biotin carboxylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ANP B K115 I155 K157 G162 G164 I167 F201 I202 E274 I276 M287 E288 K114 I154 K156 G161 G163 I166 F200 I201 E273 I275 M286 E287
BS02 MG B E274 E288 E273 E287
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003989 acetyl-CoA carboxylase activity
GO:0004075 biotin carboxylase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:2001295 malonyl-CoA biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2vpq, PDBe:2vpq, PDBj:2vpq
PDBsum2vpq
PubMed18725455
UniProtA0A0H3JRR2

[Back to BioLiP]