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PDBsum entry 1zoa

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
1zoa
Jmol
Contents
Protein chains
457 a.a. *
Ligands
HEM ×2
140 ×2
MES ×2
GOL ×2
Waters ×933
* Residue conservation analysis
PDB id:
1zoa
Name: Oxidoreductase
Title: Crystal structure of a328v mutant of the heme domain of p450 n-palmitoylglycine
Structure: Bifunctional p-450:nadph-p450 reductase. Chain: a, b. Fragment: cytochrome p450. Engineered: yes. Mutation: yes
Source: Bacillus megaterium. Organism_taxid: 1404. Gene: cyp102a1, cyp102. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.74Å     R-factor:   0.165     R-free:   0.196
Authors: A.Hegda,B.Chen,D.C.Haines,M.Bondlela,D.Mullin,S.E.Graham, D.R.Tomchick,M.Machius,J.A.Peterson
Key ref: D.C.Haines et al. (2011). A single active-site mutation of P450BM-3 dramatically enhances substrate binding and rate of product formation. Biochemistry, 50, 8333-8341. PubMed id: 21875028
Date:
12-May-05     Release date:   01-Aug-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P14779  (CPXB_BACME) -  Bifunctional P-450/NADPH-P450 reductase
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1049 a.a.
457 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 2: 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: 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  

 

 
    reference    
 
 
Biochemistry 50:8333-8341 (2011)
PubMed id: 21875028  
 
 
A single active-site mutation of P450BM-3 dramatically enhances substrate binding and rate of product formation.
D.C.Haines, A.Hegde, B.Chen, W.Zhao, M.Bondlela, J.M.Humphreys, D.A.Mullin, D.R.Tomchick, M.Machius, J.A.Peterson.
 
  ABSTRACT  
 
No abstract given.