X-ray diffraction
2.64Å resolution

Structure of succinyl-CoA: 3-ketoacid CoA transferase from Drosophila melanogaster

Source organism: Drosophila melanogaster
Primary publication:
Structure of succinyl-CoA:3-ketoacid CoA transferase from Drosophila melanogaster.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69 1089-93 (2013)
PMID: 24100554

Function and Biology Details

Reaction catalysed:
Succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Succinyl-CoA:3-ketoacid-coenzyme A transferase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 487 amino acids
Theoretical weight: 51.72 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
  • Canonical: Q9W058 (Residues: 34-516; Coverage: 94%)
Gene names: CG1140, SCOT
Sequence domains: Coenzyme A transferase
Structure domains: Glutaconate Coenzyme A-transferase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 76.638Å b: 101.921Å c: 122.457Å
α: 90° β: 90° γ: 90°
R R work R free
0.207 0.204 0.261
Expression system: Escherichia coli