› 6t6v

Electron Microscopy
4.5Å resolution

Glu-494-Ala inactive monomer of a quinol dependent Nitric Oxide Reductase (qNOR) from Alcaligenes xylosoxidans

Released:
DOI: 10.2210/pdb6t6v/pdb
PDB entry 6t6v coloured by chain, front view.
PDB entry 6t6v coloured by chain, side view.
PDB entry 6t6v coloured by chain, top view.
Source organism: Achromobacter xylosoxidans
Primary publication:
The active form of quinol-dependent nitric oxide reductase from Neisseria meningitidis is a dimer.
Jamali MAM, Gopalasingam CC, Johnson RM, Tosha T, Muramoto K, Muench SP, Antonyuk SV, Shiro Y, Hasnain SS
OpenAccess logo IUCrJ 7 404-415 (2020)
PMID: 32431824
Related structures: EMD-10387

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-244174 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nitric oxide reductase subunit B Chain: A
Molecule details ›
Chain: A
Length: 762 amino acids
Theoretical weight: 84.77 KDa
Source organism: Achromobacter xylosoxidans
Expression system: Escherichia coli BL21(DE3)

Ligands and Environments

2 bound ligands:
Ligand HEM 2 x HEM
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4.5Å
Relevant EMDB volumes: EMD-10387
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

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

2 mentions without citation

The active form of quinol-dependent nitric oxide reductase from Neisseria meningitidis is a dimer.
Jamali et al. (2020)
1 more