› 2za2

X-ray diffraction
2.7Å resolution

Crystal Structure of the apo-form of orotidine-5'-monophosphate decarboxylase from P.falciparum

Released:
DOI: 10.2210/pdb2za2/pdb
PDB entry 2za2 coloured by chain, front view.
PDB entry 2za2 coloured by chain, side view.
PDB entry 2za2 coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Structural basis for the decarboxylation of orotidine 5'-monophosphate (OMP) by Plasmodium falciparum OMP decarboxylase.
Tokuoka K, Kusakari Y, Krungkrai SR, Matsumura H, Kai Y, Krungkrai J, Horii T, Inoue T
J Biochem 143 69-78 (2008)
PMID: 17981823

Function and Biology Details

Reaction catalysed: 
Orotidine 5'-phosphate = UMP + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186132 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
orotidine-5'-phosphate decarboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 323 amino acids
Theoretical weight: 37.87 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8T6J6 (Residues: 1-323; Coverage: 100%)
Gene name: ompdc
Sequence domains: Orotidine 5'-phosphate decarboxylase / HUMPS family
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: R3
Unit cell:
a: 201.8Å b: 201.8Å c: 44Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.21 0.309
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Malaria parasite carbonic anhydrase: inhibition of aromatic/heterocyclic sulfonamides and its therapeutic potential.
Krungkrai et al. (2011)
3 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