› 4eub

X-ray diffraction
1.97Å resolution

Succinyl-CoA:acetate CoA-transferase (AarCH6-E294A) in complex with CoA

Released:
DOI: 10.2210/pdb4eub/pdb
PDB entry 4eub coloured by chain, front view.
PDB entry 4eub coloured by chain, side view.
PDB entry 4eub coloured by chain, top view.
Source organism: Acetobacter aceti
Primary publication:
Crystal structures of Acetobacter aceti succinyl-coenzyme A (CoA):acetate CoA-transferase reveal specificity determinants and illustrate the mechanism used by class I CoA-transferases.
Mullins EA, Kappock TJ
Biochemistry 51 8422-34 (2012)
PMID: 23030530

Function and Biology Details

Reaction catalysed: 
Succinyl-CoA + acetate = acetyl-CoA + succinate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109828 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Succinyl-CoA:acetate CoA-transferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 514 amino acids
Theoretical weight: 55.99 KDa
Source organism: Acetobacter aceti
Expression system: Escherichia coli
UniProt:
  • Canonical: B3EY95 (Residues: 1-505; Coverage: 100%)
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand COA 2 x COA
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 67.404Å b: 110.277Å c: 120.242Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.154 0.209
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Specificity in transition state binding: the Pauling model revisited.
Amyes et al. (2013)
1 more

2 mentions without citation

Thioesterase enzyme families: Functions, structures, and mechanisms.
Caswell et al. (2022)
1 more