X-ray diffraction
2.05Å resolution

Crystal structure of UDP-glucose pyrophosphorylase S374F mutant from Leishmania major in complex with UDP-glucose


Function and Biology Details

Reaction catalysed:
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
UTP--glucose-1-phosphate uridylyltransferase Chain: A
Molecule details ›
Chain: A
Length: 505 amino acids
Theoretical weight: 56.11 KDa
Source organism: Leishmania major
Expression system: Escherichia coli
  • Canonical: Q4QDU3 (Residues: 1-494; Coverage: 100%)
Gene names: LMJF_18_0990, UGP
Sequence domains: UTP--glucose-1-phosphate uridylyltransferase
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2221
Unit cell:
a: 79.39Å b: 88.18Å c: 137.37Å
α: 90° β: 90° γ: 90°
R R work R free
0.191 0.188 0.244
Expression system: Escherichia coli