› 1fo6

X-ray diffraction
1.95Å resolution

CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE

Released:
DOI: 10.2210/pdb1fo6/pdb
PDB entry 1fo6 coloured by chain, front view.
PDB entry 1fo6 coloured by chain, side view.
PDB entry 1fo6 coloured by chain, top view.
Source organism: Agrobacterium tumefaciens
Primary publication:
Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft.
Wang WC, Hsu WH, Chien FT, Chen CY
J Mol Biol 306 251-61 (2001)
PMID: 11237598

Function and Biology Details

Reaction catalysed: 
N-carbamoyl-D-amino acid + H(2)O = D-amino acid + NH(3) + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175013 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-carbamoyl-D-amino acid hydrolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 304 amino acids
Theoretical weight: 34.21 KDa
Source organism: Agrobacterium tumefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q44185 (Residues: 1-304; Coverage: 100%)
Sequence domains: Carbon-nitrogen hydrolase
Structure domains: Carbon-nitrogen hydrolase

Ligands and Environments

1 bound ligand:
Ligand XE 2 x XE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 70.23Å b: 67.53Å c: 137.48Å
α: 90° β: 96.12° γ: 90°
R-values:
R R work R free
0.187 not available 0.239
Expression system: Escherichia coli

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Citations

5 review citations

Nickel: Human Health and Environmental Toxicology.
Genchi et al. (2020)
4 more

3 mentions without citation

Mechanisms of nickel toxicity in microorganisms.
Macomber et al. (2011)
2 more