› 2nrc

X-ray diffraction
2.05Å resolution

C28A Mutant of Succinyl-CoA:3-Ketoacid CoA Transferase from Pig Heart

Released:
DOI: 10.2210/pdb2nrc/pdb
PDB entry 2nrc coloured by chain, front view.
PDB entry 2nrc coloured by chain, side view.
PDB entry 2nrc coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Identification of the cysteine residue exposed by the conformational change in pig heart succinyl-CoA:3-ketoacid coenzyme A transferase on binding coenzyme A.
Tammam SD, Rochet JC, Fraser ME
Biochemistry 46 10852-63 (2007)
PMID: 17718512

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

Assemblies composition:
homo dimer (preferred)
homo tetramer
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: 52.26 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli BL21(DE3)
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
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 58.3Å b: 262.4Å c: 60.7Å
α: 90° β: 109.5° γ: 90°
R-values:
R R work R free
0.233 0.231 0.272
Expression system: Escherichia coli BL21(DE3)

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Citations

6 citation in other articles

Obligate role for ketone body oxidation in neonatal metabolic homeostasis.
Cotter et al. (2011)
5 more