› 1grq

X-ray diffraction
2.9Å resolution

CHLORAMPHENICOL PHOSPHOTRANSFERASE IN COMPLEX WITH P-AMINO-CHLORAMPHENICOL FROM STREPTOMYCES VENEZUELAE

Released:
DOI: 10.2210/pdb1grq/pdb
PDB 1grq coloured by chain and viewed from the front.
PDB 1grq coloured by chain and viewed from the side.
PDB 1grq coloured by chain and viewed from the top.
Source organism: Streptomyces venezuelae
Entry author: Izard T

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chloramphenicol 3-O phosphotransferase Chain: A
Molecule details ›
Chain: A
Length: 178 amino acids
Theoretical weight: 18.83 KDa
Source organism: Streptomyces venezuelae
UniProt:
  • Canonical: Q56148 (Residues: 1-178; Coverage: 100%)
Gene name: SVEN_4064
Sequence domains: Chloramphenicol phosphotransferase-like protein
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand CLK 1 x CLK
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: I4132
Unit cell:
a: 200Å b: 200Å c: 200Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.278 0.278 0.297

Quick links

Citations

2 review citations

Crossroads of Antibiotic Resistance and Biosynthesis.
Wencewicz TA. (2019)
1 more

1 mention without citation

Structure of Deinococcus radiodurans tunicamycin-resistance protein (TmrD), a phosphotransferase.
Kapp et al. (2008)