› 3oh4

X-ray diffraction
2.21Å resolution

Protein structure of USP from L. major bound to URIDINE-5'-DIPHOSPHATE Glucose

Released:
DOI: 10.2210/pdb3oh4/pdb
PDB entry 3oh4 coloured by chain, front view.
PDB entry 3oh4 coloured by chain, side view.
PDB entry 3oh4 coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
Structural basis for the broad substrate range of the UDP-sugar pyrophosphorylase from Leishmania major.
Dickmanns A, Damerow S, Neumann P, Schulz EC, Lamerz AC, Routier FH, Ficner R
J Mol Biol 405 461-78 (2011)
PMID: 21073876

Function and Biology Details

Reaction catalysed: 
UTP + a monosaccharide 1-phosphate = diphosphate + UDP-monosaccharide
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112478 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UTP-monosaccharide-1-phosphate uridylyltransferase Chain: A
Molecule details ›
Chain: A
Length: 641 amino acids
Theoretical weight: 70.54 KDa
Source organism: Leishmania major
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D3G6S4 (Residues: 1-630; Coverage: 100%)
Gene name: USP
Sequence domains: UTP--glucose-1-phosphate uridylyltransferase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand UPG 1 x UPG
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2
Unit cell:
a: 107.814Å b: 121.665Å c: 61.393Å
α: 90° β: 105.73° γ: 90°
R-values:
R R work R free
0.18 0.178 0.212
Expression system: Escherichia coli BL21(DE3)

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Citations

6 review citations

Enzymatic methods for glyco(diversification/randomization) of drugs and small molecules.
Gantt et al. (2011)
5 more

1 mention without citation

Substrate Specificity and Inhibitor Sensitivity of Plant UDP-Sugar Producing Pyrophosphorylases.
Decker et al. (2017)