› 2xxg

X-ray diffraction
1.6Å resolution

STRUCTURE OF THE N90S MUTANT OF NITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS

Released:
DOI: 10.2210/pdb2xxg/pdb
PDB entry 2xxg coloured by chain, front view.
PDB entry 2xxg coloured by chain, side view.
PDB entry 2xxg coloured by chain, top view.
Source organism: Achromobacter xylosoxidans
Primary publication:
Identification of the proton channel to the active site type 2 Cu center of nitrite reductase: structural and enzymatic properties of the His254Phe and Asn90Ser mutants.
Hough MA, Eady RR, Hasnain SS
Biochemistry 47 13547-53 (2008)
PMID: 19053252

Function and Biology Details

Reaction catalysed: 
Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130622 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-containing nitrite reductase Chains: A, C
Molecule details ›
Chains: A, C
Length: 336 amino acids
Theoretical weight: 36.53 KDa
Source organism: Achromobacter xylosoxidans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O68601 (Residues: 25-360; Coverage: 100%)
Gene names: O9570_16215, nir, nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

5 bound ligands:
Ligand PG4 2 x PG4
Ligand CU 4 x CU
Ligand ZN 4 x ZN
Ligand PEG 4 x PEG
Ligand MES 4 x MES
1 modified residue:
Ligand PCA 2 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: R3
Unit cell:
a: 89.552Å b: 89.552Å c: 287.678Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 0.168 0.211
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Gating mechanisms for biological electron transfer: integrating structure with biophysics reveals the nature of redox control in cytochrome P450 reductase and copper-dependent nitrite reductase.
Leferink et al. (2012)
1 more

1 mention without citation

Outlier analyses of the Protein Data Bank archive using a probability-density-ranking approach.
Shao et al. (2018)