› 1l2u

X-ray diffraction
2.5Å resolution

Orotidine 5'-monophosphate decarboxylase from E. coli

Released:
DOI: 10.2210/pdb1l2u/pdb
PDB entry 1l2u coloured by chain, front view.
PDB entry 1l2u coloured by chain, side view.
PDB entry 1l2u coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Substrate binding induces domain movements in orotidine 5'-monophosphate decarboxylase.
Harris P, Poulsen JC, Jensen KF, Larsen S
J Mol Biol 318 1019-29 (2002)
PMID: 12054799

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-140061 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Orotidine 5'-phosphate decarboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 245 amino acids
Theoretical weight: 26.38 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P08244 (Residues: 1-245; Coverage: 100%)
Gene names: JW1273, b1281, pyrF
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: MAX II BEAMLINE I711
Spacegroup: P3221
Unit cell:
a: 142.69Å b: 142.69Å c: 105.37Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.162 0.159 0.211
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Orotidine 5'-Monophosphate Decarboxylase: Probing the Limits of the Possible for Enzyme Catalysis.
Richard et al. (2018)
8 other articles

3 mentions without citation

Comprehensive analysis of loops at protein-protein interfaces for macrocycle design.
Gavenonis et al. (2014)
2 more