› 1rjr

X-ray diffraction
2.1Å resolution

The crystal structure of the D-aminoacylase D366A mutant in complex with 100mM ZnCl2

Released:
DOI: 10.2210/pdb1rjr/pdb
PDB entry 1rjr coloured by chain, front view.
PDB entry 1rjr coloured by chain, side view.
PDB entry 1rjr coloured by chain, top view.
Source organism: Alcaligenes faecalis
Primary publication:
The functional role of the binuclear metal center in D-aminoacylase: one-metal activation and second-metal attenuation.
Lai WL, Chou LY, Ting CY, Kirby R, Tsai YC, Wang AH, Liaw SH
J Biol Chem 279 13962-7 (2004)
PMID: 14736882

Function and Biology Details

Reaction catalysed: 
N-acyl-D-amino acid + H(2)O = a carboxylate + D-amino acid
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189543 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amidohydrolase 3 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 496 amino acids
Theoretical weight: 53.42 KDa
Source organism: Alcaligenes faecalis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9AGH8 (Residues: 1-484; Coverage: 100%)
Sequence domains: Amidohydrolase family
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ACT 2 x ACT
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL17B2
Spacegroup: P212121
Unit cell:
a: 60.517Å b: 77.815Å c: 136.647Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.225
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Zinc hydrolases: the mechanisms of zinc-dependent deacetylases.
Hernick et al. (2005)
1 more