› 2vax

X-ray diffraction
2.6Å resolution

Crystal structure of deacetylcephalosporin C acetyltransferase (Cephalosporin C-soak)

Released:
DOI: 10.2210/pdb2vax/pdb
PDB entry 2vax coloured by chain, front view.
PDB entry 2vax coloured by chain, side view.
PDB entry 2vax coloured by chain, top view.
Source organism: Acremonium chrysogenum
Primary publication:
The last step in cephalosporin C formation revealed: crystal structures of deacetylcephalosporin C acetyltransferase from Acremonium chrysogenum in complexes with reaction intermediates.
Lejon S, Ellis J, Valegård K
J Mol Biol 377 935-44 (2008)
PMID: 18279889

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + deacetylcephalosporin C = CoA + cephalosporin C
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
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: 49.26 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

2 bound ligands:
Ligand CSC 12 x CSC
Ligand ACT 10 x ACT
1 modified residue:
Ligand OAS 12 x OAS

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21
Unit cell:
a: 121.357Å b: 109.288Å c: 195.388Å
α: 90° β: 90.03° γ: 90°
R-values:
R R work R free
0.212 0.211 0.24
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

The enzymes of β-lactam biosynthesis.
Hamed et al. (2013)
4 more

2 mentions without citation

How the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes.
Rauwerdink et al. (2015)
1 more