› 1rk5

X-ray diffraction
1.8Å resolution

The D-aminoacylase mutant D366A in complex with 100mM CuCl2

Released:
DOI: 10.2210/pdb1rk5/pdb
PDB entry 1rk5 coloured by chain, front view.
PDB entry 1rk5 coloured by chain, side view.
PDB entry 1rk5 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:
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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL17B2
Spacegroup: P212121
Unit cell:
a: 60.016Å b: 77.266Å c: 135.982Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.204
Expression system: Escherichia coli

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Citations

2 review citations

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

1 mention without citation

Unconventional isoquinoline-based SERMs elicit fulvestrant-like transcriptional programs in ER+ breast cancer cells.
Hancock et al. (2022)