› 1los

X-ray diffraction
1.9Å resolution

crystal structure of orotidine monophosphate decarboxylase mutant deltaR203A complexed with 6-azaUMP

Released:
DOI: 10.2210/pdb1los/pdb
PDB entry 1los coloured by chain, front view.
PDB entry 1los coloured by chain, side view.
PDB entry 1los coloured by chain, top view.
Source organism: Methanothermobacter thermautotrophicus str. Delta H
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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 224 amino acids
Theoretical weight: 24.47 KDa
Source organism: Methanothermobacter thermautotrophicus str. Delta H
Expression system: Escherichia coli
UniProt:
  • Canonical: O26232 (Residues: 1-228; Coverage: 98%)
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 UP6 4 x UP6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P1
Unit cell:
a: 52.49Å b: 56.152Å c: 73.87Å
α: 82.76° β: 89.89° γ: 76.91°
R-values:
R R work R free
0.205 0.205 0.24
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

2 mentions without citation

Synthesis, preliminary bioevaluation and computational analysis of caffeic acid analogues.
Liu et al. (2014)
1 more