Structure of PDB 7y0q Chain A

Receptor sequence
>7y0qA (length=443) Species: 1348623 (Priestia megaterium NBRC 15308 = ATCC 14581) [Search protein sequence]
KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQALKFVRDFTGDGLATSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRAYDENKRQFQED
IKVMNDLVDKIIADRKQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFL
LAGHEVTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLK
YVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHR
DKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATL
VLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
3D structure
PDB7y0q Crystal structure of the P450 BM3 heme domain mutant F87A/T268V/A82T/I263L in complex with p-toluidine
ChainA
Resolution2.31 Å
3D
structure
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Enzymatic activity
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 A87 W96 F261 A264 V268 A328 F331 P392 F393 R398 C400 I401 K67 L84 A85 W94 F249 A252 V256 A316 F319 P380 F381 R386 C388 I389
BS02 4MN A V268 A328 V256 A316
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:7y0q, PDBe:7y0q, PDBj:7y0q
PDBsum7y0q
PubMed
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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