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PDBsum entry 2j1m

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
2j1m
Jmol
Contents
Protein chains
454 a.a. *
Ligands
HEM ×2
DMS ×4
Metals
_ZN ×7
Waters ×955
* Residue conservation analysis
PDB id:
2j1m
Name: Oxidoreductase
Title: P450 bm3 heme domain in complex with dmso
Structure: Cytochrome p450 102. Chain: a, b,. Fragment: heme domain, residues 1-455. Synonym: p450 bm3. Engineered: yes
Source: Bacillus megaterium. Organism_taxid: 1404. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.70Å     R-factor:   0.171     R-free:   0.199
Authors: J.Kuper,W.Tuck-Seng,D.Roccatano,M.Wilmanns,U.Schwaneberg
Key ref: J.Kuper et al. (2007). Understanding a mechanism of organic cosolvent inactivation in heme monooxygenase P450 BM-3. J Am Chem Soc, 129, 5786-5787. PubMed id: 17429965 DOI: 10.1021/ja067036x
Date:
14-Aug-06     Release date:   15-May-07    
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.
454 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: 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    
 
 
DOI no: 10.1021/ja067036x J Am Chem Soc 129:5786-5787 (2007)
PubMed id: 17429965  
 
 
Understanding a mechanism of organic cosolvent inactivation in heme monooxygenase P450 BM-3.
J.Kuper, T.S.Wong, D.Roccatano, M.Wilmanns, U.Schwaneberg.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20632328 K.S.Rabe, M.Erkelenz, K.Kiko, and C.M.Niemeyer (2010).
Peroxidase activity of bacterial cytochrome P450 enzymes: modulation by fatty acids and organic solvents.
  Biotechnol J, 5, 891-899.  
19261539 A.V.Shivange, J.Marienhagen, H.Mundhada, A.Schenk, and U.Schwaneberg (2009).
Advances in generating functional diversity for directed protein evolution.
  Curr Opin Chem Biol, 13, 19-25.  
19172188 G.Colombo, M.Meli, G.Morra, R.Gabizon, and M.Gasset (2009).
Methionine sulfoxides on prion protein Helix-3 switch on the alpha-fold destabilization required for conversion.
  PLoS ONE, 4, e4296.  
18988262 J.Zhao, and K.Auclair (2009).
The activity of human CYP2D6 in low water organic solvents.
  Biotechnol Bioeng, 102, 1268-1272.  
18392864 C.K.Chen, T.K.h.Shokhireva, R.E.Berry, H.Zhang, and F.A.Walker (2008).
The effect of mutation of F87 on the properties of CYP102A1-CYP4C7 chimeras: altered regiospecificity and substrate selectivity.
  J Biol Inorg Chem, 13, 813-824.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.