Structure of PDB 1bvy Chain A

Receptor sequence
>1bvyA (length=439) Species: 1404 (Priestia megaterium) [Search protein sequence]
LNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDK
NLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMM
VDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRFNSFYRDQ
PHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKI
IADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFLIAGHETT
SGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLN
EALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGD
DVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLVLGMMLK
HFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLGGI
3D structure
PDB1bvy Structure of a cytochrome P450-redox partner electron-transfer complex.
ChainA
Resolution2.03 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) T249 F374 C381
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 A264 G265 T268 A328 F331 P392 F393 R398 C400 G402 K50 L67 F68 W77 A245 G246 T249 A309 F312 P373 F374 R379 C381 G383
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:1bvy, PDBe:1bvy, PDBj:1bvy
PDBsum1bvy
PubMed10051560
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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