› 1urr

X-ray diffraction
1.5Å resolution

A novel Drosophila Melanogaster Acylphosphatase (AcPDro2)

Released:
DOI: 10.2210/pdb1urr/pdb
PDB entry 1urr coloured by chain, front view.
PDB entry 1urr coloured by chain, side view.
PDB entry 1urr coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase.
Zuccotti S, Rosano C, Ramazzotti M, Degl'Innocenti D, Stefani M, Manao G, Bolognesi M
Acta Crystallogr D Biol Crystallogr 60 1177-9 (2004)
PMID: 15159593

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194239 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acylphosphatase-2 Chain: A
Molecule details ›
Chain: A
Length: 102 amino acids
Theoretical weight: 11.78 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9VF36 (Residues: 1-102; Coverage: 100%)
Gene names: Acyp2, CG18505
Sequence domains: Acylphosphatase
Structure domains: Alpha-Beta Plaits

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3121
Unit cell:
a: 45.722Å b: 45.722Å c: 98.585Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.163 0.16 0.23
Expression system: Escherichia coli

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Citations

1 review citation

"Native-like aggregation" of the acylphosphatase from Sulfolobus solfataricus and its biological implications.
Bemporad et al. (2009)
10 other articles

3 mentions without citation

Refining homology models by combining replica-exchange molecular dynamics and statistical potentials.
Zhu et al. (2008)
2 more