Structure of PDB 2vpq Chain B Binding Site BS02

Receptor Information

>2vpq Chain B (length=448) Species: 1280 (Staphylococcus aureus)

KKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVG
PTLSKDSYLNIPNILSIATSTGCDGVHPGYGFLAENADFAELCEACQLKF
IGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIG
YPVIIKATAGGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKF
IENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEEAPSPILDDETR
REMGNAAVRAAKAVNYENAGTIEFIYDLNDNKFYFMEMNTRIQVEHPVTE
MVTGIDLVKLQLQVAMGDVLPYKQEDIKLTGHAIEFRINAENPYKNFMPS
PGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAIM
AGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQNSIMND

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 2vpq Chain B Residue 1451

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2vpq Structural Evidence for Substrate-Induced Synergism and Half-Sites Reactivity in Biotin Carboxylase.
• Resolution: 2.1 Å
• Binding residue (original residue number in PDB): E274 E288
• Binding residue (residue number reindexed from 1): E273 E287
• Annotation score: 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.

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

External links

• PDB: RCSB:2vpq, PDBe:2vpq, PDBj:2vpq
• PDBsum: 2vpq
• PubMed: 18725455
• UniProt: A0A0H3JRR2