› 2ghr

X-ray diffraction
2.4Å resolution

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180920 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Homoserine O-acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 302 amino acids
Theoretical weight: 35.73 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q72X44 (Residues: 1-301; Coverage: 100%)
Gene names: BCE_5534, metA, metAA
Sequence domains: Homoserine O-succinyltransferase
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL1-5
Spacegroup: P4122
Unit cell:
a: 95.89Å b: 95.89Å c: 75.403Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.188 0.25
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Amino acid biosynthesis: new architectures in allosteric enzymes.
Curien et al. (2008)
4 other articles

2 mentions without citation

PSI-2: structural genomics to cover protein domain family space.
Dessailly et al. (2009)
1 more