X-ray diffraction
2.9Å resolution

Structure of CATI in complex with chloramphenicol


Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Chloramphenicol acetyltransferase Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, R, S
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, R, S
Length: 219 amino acids
Theoretical weight: 25.69 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: P62577 (Residues: 1-219; Coverage: 100%)
Gene name: cat
Sequence domains: Chloramphenicol acetyltransferase
Structure domains: Chloramphenicol acetyltransferase-like domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P1
Unit cell:
a: 107.336Å b: 114.429Å c: 114.374Å
α: 119.97° β: 97.83° γ: 98.64°
R R work R free
0.24 0.236 0.309
Expression system: Escherichia coli