› 1erz

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE OF N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE WITH A NOVEL CATALYTIC FRAMEWORK COMMON TO AMIDOHYDROLASES

Released:
DOI: 10.2210/pdb1erz/pdb
PDB entry 1erz coloured by chain, front view.
PDB entry 1erz coloured by chain, side view.
PDB entry 1erz coloured by chain, top view.
Source organism: Agrobacterium sp. KNK712
Primary publication:
Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases.
Nakai T, Hasegawa T, Yamashita E, Yamamoto M, Kumasaka T, Ueki T, Nanba H, Ikenaka Y, Takahashi S, Sato M, Tsukihara T
Structure 8 729-37 (2000)
PMID: 10903946

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-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: 34.2 KDa
Source organism: Agrobacterium sp. KNK712
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: SPRING-8 BEAMLINE BL45XU
Spacegroup: P21212
Unit cell:
a: 67.84Å b: 137.83Å c: 68.39Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.201
Expression system: Escherichia coli

Quick links

Citations

8 review citations

The nitrilase family of CN hydrolysing enzymes - a comparative study.
O'Reilly et al. (2003)
7 more

8 mentions without citation

An amino acid at position 142 in nitrilase from Rhodococcus rhodochrous ATCC 33278 determines the substrate specificity for aliphatic and aromatic nitriles.
Yeom et al. (2008)
7 more