Structure of PDB 3ben Chain B

Receptor sequence
>3benB (length=457) Species: 1348623 (Priestia megaterium NBRC 15308 = ATCC 14581) [Search protein sequence]
TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTR
YLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAH
NILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTL
DTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDE
NKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLD
DENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVD
PVPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKG
DELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKS
KKIPLGG
3D structure
PDB3ben Crystal structure of inhibitor-bound P450BM-3 reveals open conformation of substrate access channel.
ChainB
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T268 F393 C400
Catalytic site (residue number reindexed from 1) T268 F393 C400
Enzyme Commision number 1.14.14.1: unspecific monooxygenase.
1.6.2.4: NADPH--hemoprotein reductase.
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 HEM B K69 L86 F87 W96 F261 A264 T268 T269 A328 F331 P392 R398 C400 I401 G402 K69 L86 F87 W96 F261 A264 T268 T269 A328 F331 P392 R398 C400 I401 G402
BS02 LEH B V26 L75 V78 F87 A264 T436 L437 V26 L75 V78 F87 A264 T436 L437 MOAD: Kd=0.32uM
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

View graph for
Molecular Function
External links
PDB RCSB:3ben, PDBe:3ben, PDBj:3ben
PDBsum3ben
PubMed18298086
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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