› 1rjq

X-ray diffraction
1.8Å resolution

The crystal structure of the D-aminoacylase mutant D366A

Released:
DOI: 10.2210/pdb1rjq/pdb
PDB 1rjq coloured by chain and viewed from the front.
PDB 1rjq coloured by chain and viewed from the side.
PDB 1rjq coloured by chain and viewed from the top.
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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-aminoacylase 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%)
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ACT 2 x ACT
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL17B2
Spacegroup: P212121
Unit cell:
a: 60.019Å b: 76.927Å c: 135.586Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 0.202
Expression system: Escherichia coli

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Citations

2 review citations

Metal binding affinity and selectivity in metalloproteins: insights from computational studies.
Dudev et al. (2008)
1 more