PDBe 6qq5

Electron Microscopy
3.9Å resolution

Cryo-EM structure of dimeric quinol dependent nitric oxide reductase (qNOR) from Alcaligenes xylosoxidans

Released:

Function and Biology Details

Reaction catalysed:
Nitrous oxide + 2 ferricytochrome c + H(2)O = 2 nitric oxide + 2 ferrocytochrome c + 2 H(+)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nitric oxide reductase subunit B Chains: A, B
Molecule details ›
Chains: A, B
Length: 746 amino acids
Theoretical weight: 83.12 KDa
Source organism: Achromobacter xylosoxidans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0D6H8R3 (Residues: 1-746; Coverage: 98%)
Gene names: ERS451415_02175, norB_1
Sequence domains: Cytochrome C and Quinol oxidase polypeptide I

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.9Å
Relevant EMDB volumes: EMD-4618
Expression system: Escherichia coli BL21(DE3)