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6the

X-ray diffraction
2.87Å resolution

Crystal structure of core domain of four-domain heme-cupredoxin-Cu nitrite reductase from Bradyrhizobium sp. ORS 375

Released:
Model geometry
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Function and Biology Details

Reaction catalysed:
nitric oxide + Fe(III)-[cytochrome c] + H2O = Fe(II)-[cytochrome c] +nitrite + 2 H(+).
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-124699 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-containing nitrite reductase Chain: A
Molecule details ›
Chain: A
Length: 321 amino acids
Theoretical weight: 34.2 KDa
Source organism: Bradyrhizobium sp. ORS 375
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: H0SHH5 (Residues: 385-698; Coverage: 45%)
Gene name: BRAO375_2740002
Sequence domains: Multicopper oxidase

Ligands and Environments

No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: I23
Unit cell:
a: 125.141Å b: 125.141Å c: 125.141Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.225 0.234
Expression system: Escherichia coli BL21(DE3)