› 2xat

X-ray diffraction
3.2Å resolution

COMPLEX OF THE HEXAPEPTIDE XENOBIOTIC ACETYLTRANSFERASE WITH CHLORAMPHENICOL AND DESULFO-COENZYME A

Released:
DOI: 10.2210/pdb2xat/pdb
PDB entry 2xat coloured by chain, front view.
PDB entry 2xat coloured by chain, side view.
PDB entry 2xat coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Structure of the hexapeptide xenobiotic acetyltransferase from Pseudomonas aeruginosa.
Beaman TW, Sugantino M, Roderick SL
Biochemistry 37 6689-96 (1998)
PMID: 9578552

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150862 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chloramphenicol acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 212 amino acids
Theoretical weight: 23.51 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P26841 (Residues: 1-212; Coverage: 100%)
Gene names: PA0706, cat, catB7
Sequence domains: Bacterial transferase hexapeptide (six repeats)
Structure domains: Hexapeptide repeat proteins

Ligands and Environments


Cofactor: Ligand DCA 1 x DCA
1 bound ligand:
Ligand CLM 1 x CLM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P4132
Unit cell:
a: 154.8Å b: 154.8Å c: 154.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.213 0.255
Expression system: Escherichia coli BL21(DE3)

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Citations

8 review citations

Prokaryotic carbonic anhydrases.
Smith et al. (2000)
7 more

9 mentions without citation

New understanding of multidrug efflux and permeation in antibiotic resistance, persistence, and heteroresistance.
Manrique et al. (2023)
8 more