Brand  (β version)

PDB ID: 1BVY

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Ligands
Code Name Style Show Link
EDO 1,2-ethanediol PoSSuM
FMN Flavin mononucleotide PoSSuM
HEM Protoporphyrin ix containing Fe PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 1BVY   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : COMPLEX OF THE HEME AND FMN-BINDING DOMAINS OF THE CYTOCHROME P450(BM-3)
Release Data : 1999-02-23
Compound :
mol_id molecule chains
1 PROTEIN (CYTOCHROME P450 BM-3) A,B
ec: 1.14.14.1
fragment: HEME-BINDING DOMAIN
mol_id molecule chains
2 PROTEIN (CYTOCHROME P450 BM-3) F
ec: 1.14.14.1
fragment: FMN-BINDING DOMAIN
Source :
mol_id organism_scientific expression_system
1 Bacillus megaterium  (taxid:1404) Escherichia coli  (taxid:562)
expression_system_cell_line: DH5AF'IQ
expression_system_plasmid: PPROEX
other_details: SYNTHETIC GENE;
mol_id organism_scientific expression_system
2 Bacillus megaterium  (taxid:1404) Escherichia coli  (taxid:562)
expression_system_cell_line: DH5AF'IQ
expression_system_plasmid: PPROEX
other_details: SYNTHETIC GENE
Authors : Sevrioukova, I.F., Li, H., Zhang, H., Peterson, J.A., Poulos, T.L.
Keywords : FATTY ACID MONOOXYGENASE, HEMOPROTEIN, FLAVOPROTEIN, ELECTRON TRANSFER, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 2.03 Å )
Citation :

Structure of a cytochrome P450-redox partner electron-transfer complex.

Sevrioukova, I.F.,Li, H.,Zhang, H.  et al.
(1999)  Proc.Natl.Acad.Sci.USA  96 : 1863 - 1868

PubMed: 10051560
DOI: 10.1073/pnas.96.5.1863

Reaction

Chain : F
UniProt : P14779 (CPXB_PRIM2)
Reaction: EC: Evidence:
Physiological Direction:
2 oxidized [cytochrome P450] + NADPH = 2 reduced [cytochrome P450] + NADP(+) + H(+) 1.6.2.4 PubMed:11695889, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:16566047, PubMed:17077084, PubMed:1727637, PubMed:17868686, PubMed:18004886, PubMed:18020460, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028, PubMed:3106359, PubMed:7578081
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an organic molecule + reduced [NADPH--hemoprotein reductase] + O2 = an alcohol + oxidized [NADPH--hemoprotein reductase] + H2O + H(+) 1.14.14.1 PubMed:11695889, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:16566047, PubMed:17077084, PubMed:1727637, PubMed:17868686, PubMed:18004886, PubMed:18020460, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028, PubMed:3106359, PubMed:7578081
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Cofactor: Evidence: Note:
FAD ECO:0000269 | PubMed:7578081
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FMN ECO:0000269 | PubMed:10051560
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heme ECO:0000269 | PubMed:16403573
ECO:0000269 | PubMed:18721129
ECO:0000269 | PubMed:19492389
ECO:0000269 | PubMed:20180779
ECO:0000269 | PubMed:21110374
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