1g2v

X-ray diffraction
2.6Å resolution

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

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 73.017Å b: 134.361Å c: 140.901Å
α: 90° β: 98.22° γ: 90°
R-values:
R R work R free
0.217 0.215 0.242
Expression system: Escherichia coli