› 8bgw

Electron Microscopy
2.2Å resolution

CryoEM structure of quinol-dependent Nitric Oxide Reductase (qNOR) from Alcaligenes xylosoxidans at 2.2 A resolution

Released:
DOI: 10.2210/pdb8bgw/pdb
PDB entry 8bgw coloured by chain, front view.
PDB entry 8bgw coloured by chain, side view.
PDB entry 8bgw coloured by chain, top view.
Source organism: Achromobacter xylosoxidans
Primary publication:
A 2.2 Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases.
Flynn AJ, Antonyuk SV, Eady RR, Muench SP, Hasnain SS
OpenAccess logo Nat Commun 14 3416 (2023)
PMID: 37296134
Related structures: EMD-16041

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-244214 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nitric oxide reductase subunit B Chains: A, B
Molecule details ›
Chains: A, B
Length: 761 amino acids
Theoretical weight: 84.72 KDa
Source organism: Achromobacter xylosoxidans
Expression system: Escherichia coli BL21(DE3)

Ligands and Environments

6 bound ligands:
Ligand HEM 4 x HEM
Ligand FE 2 x FE
Ligand CA 2 x CA
Ligand 10M 2 x 10M
Ligand UQ1 2 x UQ1
Ligand LOP 13 x LOP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.2Å
Relevant EMDB volumes: EMD-16041
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

`Cryo-EM': electron cryomicroscopy, cryo electron microscopy or something else?
Henderson et al. (2023)