› 1x1z

X-ray diffraction
1.45Å resolution

Orotidine 5'-monophosphate decarboxylase (odcase) complexed with BMP (produced from 6-cyanoump)

Released:
DOI: 10.2210/pdb1x1z/pdb
PDB entry 1x1z coloured by chain, front view.
PDB entry 1x1z coloured by chain, side view.
PDB entry 1x1z coloured by chain, top view.
Source organism: Methanothermobacter thermautotrophicus
Primary publication:
An unprecedented twist to ODCase catalytic activity.
Fujihashi M, Bello AM, Poduch E, Wei L, Annedi SC, Pai EF, Kotra LP
J Am Chem Soc 127 15048-50 (2005)
PMID: 16248642

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127822 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Orotidine 5'-phosphate decarboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 252 amino acids
Theoretical weight: 27.38 KDa
Source organism: Methanothermobacter thermautotrophicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O26232 (Residues: 1-228; Coverage: 100%)
Gene names: MTH_129, pyrF
Sequence domains: Orotidine 5'-phosphate decarboxylase / HUMPS family
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand BMP 2 x BMP
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: P21
Unit cell:
a: 58.105Å b: 73.568Å c: 59.399Å
α: 90° β: 119.28° γ: 90°
R-values:
R R work R free
0.162 0.162 0.18
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Design of inhibitors of ODCase.
Mundra et al. (2014)
1 more

4 mentions without citation

Mechanism of OMP decarboxylation in orotidine 5'-monophosphate decarboxylase.
Hu et al. (2008)
3 more