PDBe 1uf7

X-ray diffraction
1.9Å resolution

Crystal structure of C171A/V236A Mutant of N-carbamyl-D-amino acid amidohydrolase complexed with N-carbamyl-D-valine

Released:
Source organism: Agrobacterium sp.
Entry authors: Hashimoto H, Aoki M, Shimizu T, Nakai T, Morikawa H, Ikenaka Y, Takahashi S, Sato M

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
Molecule details ›
Chains: A, B
Length: 303 amino acids
Theoretical weight: 34.14 KDa
Source organism: Agrobacterium sp.
Expression system: Escherichia coli
UniProt:
  • Canonical: P60327 (Residues: 2-304; 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
Spacegroup: P21212
Unit cell:
a: 67.452Å b: 137.696Å c: 68.024Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 0.218
Expression system: Escherichia coli