› 1lor

X-ray diffraction
1.6Å resolution

crystal structure of orotidine 5'-monophosphate complexed with BMP

Released:
DOI: 10.2210/pdb1lor/pdb
PDB entry 1lor coloured by chain, front view.
PDB entry 1lor coloured by chain, side view.
PDB entry 1lor coloured by chain, top view.
Source organism: Methanothermobacter thermautotrophicus
Primary publication:
Crystal structures of inhibitor complexes reveal an alternate binding mode in orotidine-5'-monophosphate decarboxylase.
Wu N, Pai EF
J Biol Chem 277 28080-7 (2002)
PMID: 12011084

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 Chain: A
Molecule details ›
Chain: A
Length: 228 amino acids
Theoretical weight: 24.87 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

1 bound ligand:
Ligand BMP 1 x BMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: C2221
Unit cell:
a: 58.365Å b: 103.796Å c: 73.821Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.173 0.196
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Mechanisms and free energies of enzymatic reactions.
Gao et al. (2006)
2 more

5 mentions without citation

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