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PDBsum entry 2xxf

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
2xxf

 

 

 

 

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Contents
Protein chains
335 a.a.
Ligands
PEG ×7
MES ×4
PG4 ×2
Metals
_ZN ×6
_CU ×4
Waters ×614
PDB id:
2xxf
Name: Oxidoreductase
Title: Cu metallated h254f mutant of nitrite reductase
Structure: Dissimilatory copper-containing nitrite reductase. Chain: a, b. Fragment: residues 26-360. Synonym: nitrite reductase, nir. Engineered: yes. Mutation: yes
Source: Achromobacter xylosoxidans. Organism_taxid: 85698. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.50Å     R-factor:   0.146     R-free:   0.177
Authors: M.A.Hough,R.R.Eady,S.S.Hasnain
Key ref: N.G.Leferink et al. (2011). Proton-coupled electron transfer in the catalytic cycle of Alcaligenes xylosoxidans copper-dependent nitrite reductase. Biochemistry, 50, 4121-4131. PubMed id: 21469743
Date:
10-Nov-10     Release date:   18-May-11    
Supersedes: 2jl3
PROCHECK
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 Headers
 References

Protein chains
O68601  (O68601_ALCXX) -  Copper-containing nitrite reductase from Alcaligenes xylosoxydans xylosoxydans
Seq:
Struc:
360 a.a.
335 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.1.7.2.1  - nitrite reductase (NO-forming).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: nitric oxide + Fe(III)-[cytochrome c] + H2O = Fe(II)-[cytochrome c] + nitrite + 2 H+
nitric oxide
+ Fe(III)-[cytochrome c]
+ H2O
= Fe(II)-[cytochrome c]
+ nitrite
+ 2 × H(+)
      Cofactor: Cu cation or Fe cation; FAD
Cu cation
or Fe cation
FAD
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Biochemistry 50:4121-4131 (2011)
PubMed id: 21469743  
 
 
Proton-coupled electron transfer in the catalytic cycle of Alcaligenes xylosoxidans copper-dependent nitrite reductase.
N.G.Leferink, C.Han, S.V.Antonyuk, D.J.Heyes, S.E.Rigby, M.A.Hough, R.R.Eady, N.S.Scrutton, S.S.Hasnain.
 
  ABSTRACT  
 
No abstract given.

 

 

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