X-ray diffraction
2.75Å resolution

Crystal Structure of a Phosphotransacetylase from Bacillus subtilis


Function and Biology Details

Reaction catalysed:
Acetyl-CoA + phosphate = CoA + acetyl phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Phosphate acetyltransferase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 329 amino acids
Theoretical weight: 35.17 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
  • Canonical: P39646 (Residues: 1-323; Coverage: 100%)
Gene names: BSU37660, ipa-88d, pta, ywfJ
Sequence domains: Phosphate acetyl/butaryl transferase
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P6422
Unit cell:
a: 185.207Å b: 185.207Å c: 259.414Å
α: 90° β: 90° γ: 120°
R R work R free
0.269 0.268 0.297
Expression system: Escherichia coli