Structure of PDB 4kf0 Chain A

Receptor sequence
>4kf0A (length=451) Species: 1404 (Priestia megaterium) [Search protein sequence]
KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQALKFVRDFFGDGLFTSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRPDDPAYDENKRQ
FQEDIKVMNDLVDKIIADRKASQSDDLLTHMLNGKDPETGEPLDDENIRY
QIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYK
QVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVL
IPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFA
LHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLG
G
3D structure
PDB4kf0 Key Mutations Alter the Cytochrome P450 BM3 Conformational Landscape and Remove Inherent Substrate Bias.
ChainA
Resolution1.45 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) T262 F387 C394
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 F107 F261 A264 G265 T268 F331 P392 F393 R398 C400 I401 G402 A406 K67 L84 F85 W94 F105 F255 A258 G259 T262 F325 P386 F387 R392 C394 I395 G396 A400
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:4kf0, PDBe:4kf0, PDBj:4kf0
PDBsum4kf0
PubMed23828198
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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