Structure of PDB 4hgg Chain A Binding Site BS02

Receptor Information

>4hgg Chain A (length=435) Species: 1404 (Priestia megaterium)

KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLATSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDERMQFQEDIKVMNDLVDKII
ADRKASGEQSDDLLAHMLNGKDPETGEPLDDENIRYQIITFLIAGHETTS
GLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDD
VEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLVLGMMLKH
FDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL

Ligand information

• Ligand ID: SYN
• InChI: InChI=1S/C8H8/c1-2-8-6-4-3-5-7-8/h2-7H,1H2
• InChIKey: PPBRXRYQALVLMV-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.370
  OpenEye OEToolkits 1.7.6: C=Cc1ccccc1
  ACDLabs 12.01: C=C\c1ccccc1
• Formula: C8 H8
• Name: ethenylbenzene;
  styrene
• ChEMBL: CHEMBL285235
• ZINC: ZINC000000968269
• PDB chain: 4hgg Chain A Residue 502

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4hgg P450 BM3 crystal structures reveal the role of the charged surface residue Lys/Arg184 in inversion of enantioselective styrene epoxidation.
• Resolution: 1.7 Å
• Binding residue (original residue number in PDB): A264 T268 A328
• Binding residue (residue number reindexed from 1): A244 T248 A308
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): T268 F393 C400
• Catalytic site (residue number reindexed from 1): T248 F373 C380
• Enzyme Commision number: 1.14.14.1: unspecific monooxygenase.
  1.6.2.4: NADPH--hemoprotein reductase.

Gene Ontology

Molecular Function

• GO:0004497 monooxygenase activity
• GO:0005506 iron ion binding
• GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
• GO:0020037 heme binding

External links

• PDB: RCSB:4hgg, PDBe:4hgg, PDBj:4hgg
• PDBsum: 4hgg
• PubMed: 23589805
• UniProt: P14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)