PDBe 1fo6

X-ray diffraction
1.95Å resolution

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

Released:

Function and Biology Details

Reaction catalysed:
N-carbamoyl-D-amino acid + H(2)O = D-amino acid + NH(3) + CO(2). 
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (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: Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase

Ligands and Environments

1 bound ligand:

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