Structure of PDB 3cbd Chain A

Receptor sequence
>3cbdA (length=455) Species: 1404 (Priestia megaterium) [Search protein sequence]
TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTR
YLSSQRLIKEACDESRFDKNLSQALKFARDFAGDGLFTSWTHEKNWKKAH
NILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEYIEVPEDMTRLTL
DTIGLCGFNYRFNSFYRDQPHPFIISMIRALDEVMNKLQRANPDDPAYDE
NKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTQMLNGKDPETGEPLD
DGNISYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKVAEEATRVLVD
PVPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKG
DEVMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKS
KKIPL
3D structure
PDB3cbd Directed Evolution of cytochrome P450 BM3, to octane monoxygenase 139-3
ChainA
Resolution2.65 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 A K69 L86 F87 W96 F261 A264 G265 T268 T269 A328 F331 P392 F393 R398 C400 I401 G402 A406 K69 L86 F87 W96 F261 A264 G265 T268 T269 A328 F331 P392 F393 R398 C400 I401 G402 A406
BS02 140 A L29 R47 Y51 F87 L188 T260 L29 R47 Y51 F87 L188 T260 BindingDB: Kd=82nM
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:3cbd, PDBe:3cbd, PDBj:3cbd
PDBsum3cbd
PubMed
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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