3cdk

X-ray diffraction
2.59Å resolution

Crystal structure of the co-expressed succinyl-CoA transferase A and B complex from Bacillus subtilis

Released:
Source organism: Bacillus subtilis
Entry authors: Kim Y, Zhou M, Stols L, Eschenfeldt W, Donnelly M, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
Succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-154606 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Probable succinyl-CoA:3-ketoacid coenzyme A transferase subunit A Chains: A, C
Molecule details ›
Chains: A, C
Length: 241 amino acids
Theoretical weight: 25.7 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P42315 (Residues: 1-238; Coverage: 100%)
Gene names: BSU38990, N15K, scoA, yxjD
Sequence domains: Coenzyme A transferase
Structure domains: Glutaconate Coenzyme A-transferase
Probable succinyl-CoA:3-ketoacid coenzyme A transferase subunit B Chains: B, D
Molecule details ›
Chains: B, D
Length: 219 amino acids
Theoretical weight: 23.63 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P42316 (Residues: 1-216; Coverage: 100%)
Gene names: BSU38980, N15L, scoB, yxjE
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: APS BEAMLINE 19-ID
Spacegroup: P2
Unit cell:
a: 69.337Å b: 70.404Å c: 97.996Å
α: 90° β: 106.31° γ: 90°
R-values:
R R work R free
0.196 0.193 0.253
Expression system: Escherichia coli BL21(DE3)