spacer
spacer

PDBsum entry 3dgi

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3dgi
Jmol
Contents
Protein chains
449 a.a. *
425 a.a. *
Ligands
HEM-DMS ×2
Waters ×508
* Residue conservation analysis
PDB id:
3dgi
Name: Oxidoreductase
Title: Crystal structure of f87a/t268a mutant of cyp bm3
Structure: Bifunctional p-450/NADPH-p450 reductase. Chain: a, b. Fragment: cytochrome p450 102, heme domain: residues 2-456. Synonym: cytochrome p450(bm-3), p450bm-3 [full length protein includes: cytochrome p450 102 (ec 1.14.14.1) and NADPH-cytochrome p450 reductase (ec 1.6.2.4)]. Engineered: yes. Mutation: yes
Source: Bacillus megaterium. Organism_taxid: 1404. Gene: cyp102a1, cyp102. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.95Å     R-factor:   0.179     R-free:   0.220
Authors: I.Le Trong,J.H.Katayama,R.A.Totah,R.E.Stenkamp,E.P.Fox
Date:
13-Jun-08     Release date:   16-Jun-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P14779  (CPXB_BACME) -  Bifunctional P-450/NADPH-P450 reductase
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1049 a.a.
449 a.a.*
Protein chain
Pfam   ArchSchema ?
P14779  (CPXB_BACME) -  Bifunctional P-450/NADPH-P450 reductase
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1049 a.a.
425 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: Chains A, B: E.C.1.14.14.1  - Unspecific monooxygenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
RH
+ reduced flavoprotein
+ O(2)
= ROH
+ oxidized flavoprotein
+ H(2)O
      Cofactor: Heme-thiolate
   Enzyme class 3: Chains A, B: E.C.1.6.2.4  - NADPH--hemoprotein reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
NADPH
+ n oxidized hemoprotein
= NADP(+)
+ n reduced hemoprotein
      Cofactor: FAD; FMN
FAD
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
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   1 term 
  Biochemical function     oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen     3 terms