› 1m3e

X-ray diffraction
2.5Å resolution

Succinyl-COA:3-ketoacid COA transferase from pig heart (selenomethionine)

Released:
DOI: 10.2210/pdb1m3e/pdb
PDB entry 1m3e coloured by chain, front view.
PDB entry 1m3e coloured by chain, side view.
PDB entry 1m3e coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Structure of the mammalian CoA transferase from pig heart.
Bateman KS, Brownie ER, Wolodko WT, Fraser ME
Biochemistry 41 14455-62 (2002)
PMID: 12463743

Function and Biology Details

Reaction catalysed: 
Succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173354 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 481 amino acids
Theoretical weight: 52.9 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q29551 (Residues: 40-520; Coverage: 93%)
Gene names: OXCT, OXCT1, SCOT
Sequence domains: Coenzyme A transferase
Structure domains: Glutaconate Coenzyme A-transferase

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 52 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P21
Unit cell:
a: 60.168Å b: 264.323Å c: 62.688Å
α: 90° β: 111.88° γ: 90°
R-values:
R R work R free
0.246 0.221 0.265
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Acetate formation in the energy metabolism of parasitic helminths and protists.
Tielens et al. (2010)
11 other articles

2 mentions without citation

Protein subunit interfaces: heterodimers versus homodimers.
Zhanhua et al. (2005)
1 more