› 5nzk

X-ray diffraction
2.45Å resolution

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

Released:
DOI: 10.2210/pdb5nzk/pdb
PDB entry 5nzk coloured by chain, front view.
PDB entry 5nzk coloured by chain, side view.
PDB entry 5nzk coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
Decoding Allosteric Networks in Biocatalysts: Rational Approach to Therapies and Biotechnologies
Cramer JT, Fuehring JI, Baruch P, Bruetting C, Knoelker H-J, Gerardy-Schahn R, Fedorov R
ACS Catalysis 8 (2018)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175696 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UTP--glucose-1-phosphate uridylyltransferase Chain: A
Molecule details ›
Chain: A
Length: 505 amino acids
Theoretical weight: 56.05 KDa
Source organism: Leishmania major
Expression system: Escherichia coli
UniProt:
  • 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:
Ligand PHE 1 x PHE
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2221
Unit cell:
a: 72.655Å b: 107.381Å c: 151.196Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.234
Expression system: Escherichia coli

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