› 2vh7

X-ray diffraction
1.45Å resolution

Crystal structure of human common-type acylphosphatase

Released:
DOI: 10.2210/pdb2vh7/pdb
PDB entry 2vh7 coloured by chain, front view.
PDB entry 2vh7 coloured by chain, side view.
PDB entry 2vh7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A rigidifying salt-bridge favors the activity of thermophilic enzyme at high temperatures at the expense of low-temperature activity.
Lam SY, Yeung RC, Yu TH, Sze KH, Wong KB
PLoS Biol 9 e1001027 (2011)
PMID: 21423654

Function and Biology Details

Reaction catalysed: 
An acylphosphate + H(2)O = a carboxylate + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139497 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acylphosphatase-1 Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 11.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07311 (Residues: 1-99; Coverage: 100%)
Gene names: ACYP1, ACYPE
Sequence domains: Acylphosphatase
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 42.577Å b: 47.235Å c: 57.261Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.228
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Defying the activity-stability trade-off in enzymes: taking advantage of entropy to enhance activity and thermostability.
Siddiqui KS. (2017)
1 more

7 mentions without citation

A rigidifying salt-bridge favors the activity of thermophilic enzyme at high temperatures at the expense of low-temperature activity.
Lam et al. (2011)
6 more