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PDBsum entry 3ojw

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protein ligands links
Oxidoreductase PDB id
3ojw
Jmol
Contents
Protein chain
609 a.a. *
Ligands
FMN
FAD
Waters ×216
* Residue conservation analysis
PDB id:
3ojw
Name: Oxidoreductase
Title: Disulfide crosslinked cytochrome p450 reductase inactive
Structure: NADPH-cytochrome p450 reductase. Chain: a. Fragment: n-terminal deletion, unp residues 57-678. Synonym: cpr, p450r. Engineered: yes. Mutation: yes
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: cypor, por. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.20Å     R-factor:   0.205     R-free:   0.251
Authors: C.Xia,D.Hamdane,A.Shen,V.Choi,C.Kasper,H.Zhang,S.-C.Im,L.Was J.P.Kim
Key ref: C.Xia et al. (2011). Conformational changes of NADPH-cytochrome P450 oxidoreductase are essential for catalysis and cofactor binding. J Biol Chem, 286, 16246-16260. PubMed id: 21345800 DOI: 10.1074/jbc.M111.230532
Date:
23-Aug-10     Release date:   23-Feb-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00388  (NCPR_RAT) -  NADPH--cytochrome P450 reductase
Seq:
Struc:
 
Seq:
Struc:
678 a.a.
609 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 8 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: 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
Bound ligand (Het Group name = FAD) corresponds exactly
FMN
Bound ligand (Het Group name = FMN) corresponds exactly
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     4 terms  

 

 
    reference    
 
 
DOI no: 10.1074/jbc.M111.230532 J Biol Chem 286:16246-16260 (2011)
PubMed id: 21345800  
 
 
Conformational changes of NADPH-cytochrome P450 oxidoreductase are essential for catalysis and cofactor binding.
C.Xia, D.Hamdane, A.L.Shen, V.Choi, C.B.Kasper, N.M.Pearl, H.Zhang, S.C.Im, L.Waskell, J.J.Kim.
 
  ABSTRACT  
 
No abstract given.