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X-ray diffraction
1.27Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189083 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acylphosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 101 amino acids
Theoretical weight: 11.65 KDa
Source organism: Saccharolobus solfataricus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q97ZL0 (Residues: 1-101; Coverage: 100%)
Gene names: SSO0887, acyP
Sequence domains: Acylphosphatase
Structure domains: Alpha-Beta Plaits

Ligands and Environments

3 bound ligands:
Ligand CD 6 x CD
Ligand CL 2 x CL
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P1
Unit cell:
a: 26.188Å b: 36.775Å c: 45.984Å
α: 81.97° β: 77.37° γ: 72.37°
R-values:
R R work R free
0.141 0.138 0.171
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Protein dynamism and evolvability.
Tokuriki et al. (2009)
1 more

4 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)
3 more