1uf4

X-ray diffraction
2.15Å resolution

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

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)
PDBe Complex ID:
PDB-CPX-157995 (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: Carbon-nitrogen hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21212
Unit cell:
a: 67.264Å b: 136.848Å c: 67.762Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.201 0.256
Expression system: Escherichia coli