Your browser does not support inline frames or is currently configured not to display inline frames. Content can be viewed at actual source page: inc/head.html
PDBsum entry 2xxf
Go to PDB code:
Oxidoreductase
PDB id
2xxf
Loading ...
Contents
Protein chains
335 a.a.
Ligands
PEG
×7
MES
×4
PG4
×2
Metals
_ZN
×6
_CU
×4
Waters
×614
PDB id:
2xxf
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
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
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.
'); } }