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PDBsum entry 4z2t

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
4z2t

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
559 a.a.
Ligands
FAD ×2
Waters ×455
PDB id:
4z2t
Name: Oxidoreductase
Title: Crystal structure of 2-hydroxybiphenyl 3-monooxygenase w225y from pseudomonas azelaica
Structure: 2-hydroxybiphenyl-3-monooxygenase. Chain: a, b. Engineered: yes. Mutation: yes
Source: Pseudomonas nitroreducens hbp1. Organism_taxid: 1437882. Gene: hbpa. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.45Å     R-factor:   0.219     R-free:   0.236
Authors: M.Kanteev,A.Bregman-Cohen,A.Fishman
Key ref: M.Kanteev et al. (2015). A crystal structure of 2-hydroxybiphenyl 3-monooxygenase with bound substrate provides insights into the enzymatic mechanism. Biochim Biophys Acta, 1854, 1906-1913. PubMed id: 26275805 DOI: 10.1016/j.bbapap.2015.08.002
Date:
30-Mar-15     Release date:   19-Aug-15    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O06647  (O06647_PSENT) -  2-hydroxybiphenyl-3-monooxygenase from Pseudomonas nitroreducens
Seq:
Struc:
 
Seq:
Struc:
586 a.a.
559 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.1.14.13.44  - 2-hydroxybiphenyl 3-monooxygenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: biphenyl-2-ol + NADH + O2 + H+ = biphenyl-2,3-diol + NAD+ + H2O
biphenyl-2-ol
+ NADH
+
O2
Bound ligand (Het Group name = FAD)
matches with 76.36% similarity
+ H(+)
= biphenyl-2,3-diol
+ NAD(+)
+ H2O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1016/j.bbapap.2015.08.002 Biochim Biophys Acta 1854:1906-1913 (2015)
PubMed id: 26275805  
 
 
A crystal structure of 2-hydroxybiphenyl 3-monooxygenase with bound substrate provides insights into the enzymatic mechanism.
M.Kanteev, A.Bregman-Cohen, B.Deri, A.Shahar, N.Adir, A.Fishman.
 
  ABSTRACT  
 
No abstract given.

 

 

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