Structure of PDB 1bvy Chain B

Receptor sequence
>1bvyB (length=438) Species: 1404 (Priestia megaterium) [Search protein sequence]
NTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKN
LSQALKFVRDFAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMV
DIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRFNSFYRDQP
HPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKII
ADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFLIAGHETTS
GLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDD
VEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLVLGMMLKH
FDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLGGI
3D structure
PDB1bvy Structure of a cytochrome P450-redox partner electron-transfer complex.
ChainB
Resolution2.03 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 B K69 W96 A264 G265 T268 F331 P392 F393 R398 C400 G402 K49 W76 A244 G245 T248 F311 P372 F373 R378 C380 G382
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)

[Back to BioLiP]