1h5t

X-ray diffraction
1.9Å resolution

Thymidylyltransferase complexed with Thymidylyldiphosphate-glucose

Released:
Source organism: Escherichia coli
Entry authors: Rosano C, Zuccotti S, Bolognesi M

Function and Biology Details

Reaction catalysed:
dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-alpha-D-glucose
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glucose-1-phosphate thymidylyltransferase 1 Chains: A, C, D
Molecule details ›
Chains: A, C, D
Length: 293 amino acids
Theoretical weight: 32.73 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P37744 (Residues: 1-293; Coverage: 100%)
Gene names: JW2024, b2039, rfbA, rmlA, rmlA1
Sequence domains: Nucleotidyl transferase
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
Glucose-1-phosphate thymidylyltransferase 1 Chain: B
Molecule details ›
Chain: B
Length: 293 amino acids
Theoretical weight: 32.71 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P37744 (Residues: 1-293; Coverage: 100%)
Gene names: JW2024, b2039, rfbA, rmlA, rmlA1
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 ID14-2
Spacegroup: P21
Unit cell:
a: 72.81Å b: 119.49Å c: 81.17Å
α: 90° β: 112.67° γ: 90°
R-values:
R R work R free
0.174 0.174 0.224
Expression system: Escherichia coli