› 3qw4

X-ray diffraction
3Å resolution

Function and Biology Details

Reaction catalysed: 
Orotidine 5'-phosphate = UMP + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124904 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Orotidine 5'-phosphate decarboxylase domain-containing protein Chains: B, C
Molecule details ›
Chains: B, C
Length: 453 amino acids
Theoretical weight: 49.29 KDa
Source organism: Leishmania donovani
Expression system: Escherichia coli
UniProt:
  • Canonical: H9ABT8 (Residues: 1-452; Coverage: 99%)
Gene names: CGC21_25085, LDBPK_160560
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand U5P 3 x U5P
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P43212
Unit cell:
a: 64.722Å b: 64.722Å c: 477.596Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.236 0.304
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Recent developments in drug discovery for leishmaniasis and human African trypanosomiasis.
Nagle et al. (2014)
5 more

2 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
1 more