X-ray diffraction
1.84Å resolution

Structural insights into the substrate selectivity of acyl-CoA transferase

Entry authors: Chang HY, Ko TP

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
2-amino-3-ketobutyrate coenzyme A ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 400 amino acids
Theoretical weight: 43.73 KDa
Source organism: Vibrio proteolyticus NBRC 13287
Expression system: Escherichia coli
  • Canonical: U3BPN5 (Residues: 1-398; Coverage: 100%)
Gene names: VPR01S_15_00210, kbl
Sequence domains: Aminotransferase class I and II

Ligands and Environments

Cofactor: Ligand PLP 1 x PLP
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL15A1
Spacegroup: P212121
Unit cell:
a: 62.724Å b: 122.63Å c: 136.462Å
α: 90° β: 90° γ: 90°
R R work R free
0.187 0.185 0.226
Expression system: Escherichia coli