2vat

X-ray diffraction
2.2Å resolution

Crystal structure of deacetylcephalosporin C acetyltransferase in complex with coenzyme A

Released:

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + deacetylcephalosporin C = CoA + cephalosporin C
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-153812 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyl-CoA--deacetylcephalosporin C acetyltransferase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 444 amino acids
Theoretical weight: 49.22 KDa
Source organism: Acremonium chrysogenum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P39058 (Residues: 1-444; Coverage: 100%)
Gene name: CEFG
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments


Cofactor: Ligand COA 12 x COA
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1, MAX II BEAMLINE I911-3
Spacegroup: P21
Unit cell:
a: 121.959Å b: 109.278Å c: 197.001Å
α: 90° β: 90.23° γ: 90°
R-values:
R R work R free
0.201 0.2 0.23
Expression system: Escherichia coli BL21(DE3)