3eev

X-ray diffraction
2.61Å resolution

Crystal Structure of Chloramphenicol Acetyltransferase VCA0300 from Vibrio cholerae O1 biovar eltor

Released:
Entry authors: Kim Y, Maltseva N, Kwon K, Anderson WF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

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-191964 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chloramphenicol acetyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 212 amino acids
Theoretical weight: 23.85 KDa
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9KMN1 (Residues: 1-209; Coverage: 100%)
Gene name: VC_A0300
Sequence domains: Bacterial transferase hexapeptide (six repeats)
Structure domains: Hexapeptide repeat proteins

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P3121
Unit cell:
a: 99.972Å b: 99.972Å c: 127.374Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.175 0.242
Expression system: Escherichia coli