› 1rzq

X-ray diffraction
2.2Å resolution

Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase from Achromobacter Cycloclastes at pH5.0

Released:
DOI: 10.2210/pdb1rzq/pdb
PDB entry 1rzq coloured by chain, front view.
PDB entry 1rzq coloured by chain, side view.
PDB entry 1rzq coloured by chain, top view.
Source organism: Achromobacter cycloclastes
Primary publication:
pH-profile crystal structure studies of C-terminal despentapeptide nitrite reductase from Achromobacter cycloclastes.
Li HT, Wang C, Chang T, Chang WC, Liu MY, Le Gall J, Gui LL, Zhang JP, An XM, Chang WR
Biochem Biophys Res Commun 316 107-13 (2004)
PMID: 15003518

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 domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150327 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-containing nitrite reductase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 335 amino acids
Theoretical weight: 36.54 KDa
Source organism: Achromobacter cycloclastes
Expression system: Escherichia coli
UniProt:
  • Canonical: P25006 (Residues: 39-373; Coverage: 99%)
Gene name: nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

3 bound ligands:
Ligand CU 6 x CU
Ligand SO4 5 x SO4
Ligand ACY 4 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CONVENTIONAL Cu
Spacegroup: P212121
Unit cell:
a: 99.02Å b: 117.44Å c: 122.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 0.208
Expression system: Escherichia coli

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Citations

2 citation in other articles

Comparative analysis of amino acid composition in the active site of nirk gene encoding copper-containing nitrite reductase (CuNiR) in bacterial spp.
Adhikari et al. (2017)
1 more