Structure of PDB 4zf8 Chain A

Receptor sequence
>4zf8A (length=460) Species: 1404 (Priestia megaterium) [Search protein sequence]
TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGLVTR
YLSSQRLIKEACDESRFDKNLSQALKFVRDIAGDGLVTSWTHEKNWKKAH
NILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTL
DTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKQQRANPDDPAYDE
NKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLD
DENIRYQIITFLIAGHVTTSGLLSFALYFLVKNPHVLQKAAEEAARVLVD
PVPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKG
DELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKS
KKIPLGGIPS
3D structure
PDB4zf8 Effect of Mutation and Substrate Binding on the Stability of Cytochrome P450BM3 Variants.
ChainA
Resolution2.766 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 V87 W96 F107 F261 A264 G265 T268 A328 F331 P392 F393 R398 C400 I401 G402 A406 K69 L86 V87 W96 F107 F261 A264 G265 T268 A328 F331 P392 F393 R398 C400 I401 G402 A406
BS02 MYT A L181 A264 T268 L181 A264 T268
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:4zf8, PDBe:4zf8, PDBj:4zf8
PDBsum4zf8
PubMed27267136
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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