PDBe 1q7l

X-ray diffraction
1.4Å resolution

Zn-binding domain of the T347G mutant of human aminoacylase-I

Released:

Function and Biology Details

Reaction catalysed:
(1) An N-acyl-aliphatic-L-amino acid + H(2)O = an aliphatic L-amino acid + a carboxylate. (2) An N-acetyl-L-cysteine-S-conjugate + H(2)O = an L-cysteine-S- conjugate + acetate. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aminoacylase-1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 198 amino acids
Theoretical weight: 22.56 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q03154 (Residues: 1-198; Coverage: 49%)
Gene name: ACY1
Structure domains: Zn peptidases
Aminoacylase-1 Chains: B, D
Molecule details ›
Chains: B, D
Length: 88 amino acids
Theoretical weight: 9.79 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q03154 (Residues: 321-408; Coverage: 22%)
Gene name: ACY1

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P212121
Unit cell:
a: 53.528Å b: 67.249Å c: 146.479Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.133 0.133 0.172
Expression system: Spodoptera frugiperda