› 4o65

X-ray diffraction
1.8Å resolution

Crystal structure of the cupredoxin domain of amoB from Nitrosocaldus yellowstonii

Released:
DOI: 10.2210/pdb4o65/pdb
PDB 4o65 coloured by chain and viewed from the front.
PDB 4o65 coloured by chain and viewed from the side.
PDB 4o65 coloured by chain and viewed from the top.
Source organism: Candidatus Nitrosocaldus yellowstonensis
Primary publication:
Structural conservation of the B subunit in the ammonia monooxygenase/particulate methane monooxygenase superfamily.
Lawton TJ, Ham J, Sun T, Rosenzweig AC
Proteins (2014)
PMID: 24523098

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative archaeal ammonia monooxygenase subunit B Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.16 KDa
Source organism: Candidatus Nitrosocaldus yellowstonensis
Expression system: Escherichia coli
UniProt:
  • Canonical: B0LKZ4 (Residues: 31-186; Coverage: 75%)
Gene name: amoB
Structure domains: Particulate methane monooxygenase, b subunit. Chain: A, domain 1

Ligands and Environments

2 bound ligands:
Ligand CU 1 x CU
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P43212
Unit cell:
a: 47.886Å b: 47.886Å c: 192.614Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.229
Expression system: Escherichia coli

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Citations

4 review citations

Ammonia oxidation: Ecology, physiology, biochemistry and why they must all come together.
Lehtovirta-Morley LE. (2018)
3 more

1 mention without citation

Structural conservation of the B subunit in the ammonia monooxygenase/particulate methane monooxygenase superfamily.
Lawton et al. (2014)