PDBsum entry 4dql

Oxidoreductase

PDB id

4dql

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Contents

			Protein chains

					378 a.a.

			Ligands

					FAD ×2


					NAP ×2


					SO4 ×2


					1PE


					PG4 ×3

			Waters ×717

PDB id:

4dql

Links

Name:

Oxidoreductase

Title:

Crystal structure of the fad binding domain of cytochrome p450 bm3 in complex with NADP+

Structure:

Bifunctional p-450/NADPH-p450 reductase. Chain: a, b. Fragment: cytochrome p450 bm3,unp residues 657-1049. Synonym: cytochrome p450(bm-3), cytochrome p450bm-3, cytochrome p450 102, NADPH--cytochrome p450 reductase. Engineered: yes

Source:

Bacillus megaterium. Organism_taxid: 1404. Gene: cyp102a1, cyp102. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.15Å

R-factor:

0.192

R-free:

0.226

Authors:

M.G.Joyce,D.Leys

Key ref:

M.G.Joyce et al. (2012). The crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3. Febs J, 279, 1694-1706. PubMed id: 22356131

Date:

16-Feb-12

Release date:

07-Mar-12

PROCHECK

	Headers

	References

Protein chains

P14779 (CPXB_PRIM2) - Bifunctional cytochrome P450/NADPH--P450 reductase from Priestia megaterium (strain ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19)

Seq: Struc:

Seq: Struc:

Seq: Struc:					1049 a.a. 378 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class 2:

E.C.1.14.14.1 - unspecific monooxygenase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

an organic molecule + reduced [NADPH--hemoprotein reductase] + O2 = an alcohol + oxidized [NADPH--hemoprotein reductase] + H2O + H⁺

organic molecule	+	reduced [NADPH--hemoprotein reductase]	+	O2	=	alcohol	+	oxidized [NADPH--hemoprotein reductase]	+	H2O	+	H(+)

Cofactor:

Heme-thiolate

Enzyme class 3:

E.C.1.6.2.4 - NADPH--hemoprotein reductase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

2 oxidized [cytochrome P450] + NADPH = 2 reduced [cytochrome P450] + NADP⁺ + H⁺

2 × oxidized [cytochrome P450]	+	NADPH	=	2 × reduced [cytochrome P450]	+	NADP(+)	+	H(+)

Cofactor:

FAD; FMN

FAD
Bound ligand (Het Group name = FAD) corresponds exactly

FMN

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

	Febs J 279:1694-1706 (2012)
PubMed id: 22356131

The crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3.
M.G.Joyce, I.S.Ekanem, O.Roitel, A.J.Dunford, R.Neeli, H.M.Girvan, G.J.Baker, R.A.Curtis, A.W.Munro, D.Leys.

ABSTRACT

No abstract given.