1g0r

X-ray diffraction
1.87Å resolution

THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). THYMIDINE/GLUCOSE-1-PHOSPHATE COMPLEX.

Released:

Function and Biology Details

Reaction catalysed:
dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-alpha-D-glucose
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-190948 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose-1-phosphate thymidylyltransferase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 293 amino acids
Theoretical weight: 32.49 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HU22 (Residues: 1-293; Coverage: 100%)
Gene names: PA5163, rmlA
Sequence domains: Nucleotidyl transferase
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P1
Unit cell:
a: 71.274Å b: 73.084Å c: 133.652Å
α: 89.98° β: 81.42° γ: 81.56°
R-values:
R R work R free
0.151 0.147 0.221
Expression system: Escherichia coli