› 6qq5

Electron Microscopy
3.9Å resolution

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

Released:
DOI: 10.2210/pdb6qq5/pdb
PDB entry 6qq5 coloured by chain, front view.
PDB entry 6qq5 coloured by chain, side view.
PDB entry 6qq5 coloured by chain, top view.
Source organism: Achromobacter xylosoxidans
Primary publication:
Dimeric structures of quinol-dependent nitric oxide reductases (qNORs) revealed by cryo-electron microscopy.
Gopalasingam CC, Johnson RM, Chiduza GN, Tosha T, Yamamoto M, Shiro Y, Antonyuk SV, Muench SP, Hasnain SS
Sci Adv 5 eaax1803 (2019)
PMID: 31489376
Related structures: EMD-4618

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101142 (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:
Ligand FE 2 x FE
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

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

Quick links

Citations

3 citation in other articles

Biochemical and crystallographic studies of monomeric and dimeric bovine cytochrome c oxidase.
Shinzawa-Itoh et al. (2021)
2 more

3 mentions without citation

Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.
Reed et al. (2021)
2 more