Structure of PDB 2vpq Chain B Binding Site BS01

Receptor Information

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

KKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVG
PTLSKDSYLNIPNILSIATSTGCDGVHPGYGFLAENADFAELCEACQLKF
IGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIG
YPVIIKATAGGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKF
IENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEEAPSPILDDETR
REMGNAAVRAAKAVNYENAGTIEFIYDLNDNKFYFMEMNTRIQVEHPVTE
MVTGIDLVKLQLQVAMGDVLPYKQEDIKLTGHAIEFRINAENPYKNFMPS
PGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAIM
AGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQNSIMND

Ligand information

• Ligand ID: ANP
• InChI: InChI=1S/C10H17N6O12P3/c11-8-5-9(13-2-12-8)16(3-14-5)10-7(18)6(17)4(27-10)1-26-31(24,25)28-30(22,23)15-29(19,20)21/h2-4,6-7,10,17-18H,1H2,(H,24,25)(H2,11,12,13)(H4,15,19,20,21,22,23)/t4-,6-,7-,10-/m1/s1
• InChIKey: PVKSNHVPLWYQGJ-KQYNXXCUSA-N
• SMILES:
  OpenEye OEToolkits 1.7.0: c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N
  CACTVS 3.370: Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)N[P](O)(O)=O)[CH](O)[CH]3O
  CACTVS 3.370: Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(=O)N[P](O)(O)=O)[C@@H](O)[C@H]3O
  ACDLabs 12.01: O=P(O)(O)NP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
  OpenEye OEToolkits 1.7.0: c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(NP(=O)(O)O)O)O)O)N
• Formula: C10 H17 N6 O12 P3
• Name: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
• ChEMBL: CHEMBL1230989
• ZINC: ZINC000008660410
• PDB chain: 2vpq Chain B Residue 1450

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): K115 I155 K157 G162 G164 I167 F201 I202 E274 I276 M287 E288
• Binding residue (residue number reindexed from 1): K114 I154 K156 G161 G163 I166 F200 I201 E273 I275 M286 E287
• Annotation score: 3

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