Structure of PDB 4key Chain B

Receptor sequence
>4keyB (length=442) Species: 1404 (Priestia megaterium) [Search protein sequence]
KEMPQPKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLI
KEACDESRFDKNLSQALKFVRDFFGDGLVTSWTHEKNWKKAHNILLPSFS
QQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGF
NYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQED
IKVMNDLVDKIIADRKSDDLLTHMLNGKDPETGEPLDDENIRYQIITFLI
AGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKY
VGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRD
KTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLV
LGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
3D structure
PDB4key Key Mutations Alter the Cytochrome P450 BM3 Conformational Landscape and Remove Inherent Substrate Bias.
ChainB
Resolution2.05 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) T255 F380 C387
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 V87 W96 F107 F261 G265 T268 T269 F331 P392 F393 G394 R398 C400 I401 A406 K61 L78 V79 W88 F99 F248 G252 T255 T256 F318 P379 F380 G381 R385 C387 I388 A393
BS02 1C6 B V26 A264 P329 L437 V18 A251 P316 L424 MOAD: Kd=0.212uM
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:4key, PDBe:4key, PDBj:4key
PDBsum4key
PubMed23828198
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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