1pd5

X-ray diffraction
2.5Å resolution

Crystal structure of E.coli chloramphenicol acetyltransferase type I at 2.5 Angstrom resolution

Released:
Source organism: Escherichia coli
Entry authors: Roidis A, Kokkinidis M

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + chloramphenicol = CoA + chloramphenicol 3-acetate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-158650 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chloramphenicol 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: 219 amino acids
Theoretical weight: 25.69 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P62577 (Residues: 1-219; Coverage: 100%)
Gene name: cat
Sequence domains: Chloramphenicol acetyltransferase
Structure domains: Chloramphenicol acetyltransferase-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 115.739Å b: 129.702Å c: 117.984Å
α: 90° β: 108.38° γ: 90°
R-values:
R R work R free
0.199 0.195 0.281
Expression system: Escherichia coli