› 1eix

X-ray diffraction
2.5Å resolution

STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM E. COLI, CO-CRYSTALLISED WITH THE INHIBITOR BMP

Released:
DOI: 10.2210/pdb1eix/pdb
PDB entry 1eix coloured by chain, front view.
PDB entry 1eix coloured by chain, side view.
PDB entry 1eix coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase.
Harris P, Navarro Poulsen JC, Jensen KF, Larsen S
Biochemistry 39 4217-24 (2000)
PMID: 10757968

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, C, D
Molecule details ›
Chains: A, B, C, D
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

1 bound ligand:
Ligand BMQ 4 x BMQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P212121
Unit cell:
a: 61.28Å b: 95.92Å c: 145.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.191 0.264
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies.
Gerlt et al. (2001)
6 more

4 mentions without citation

Surprises and pitfalls arising from (pseudo)symmetry.
Zwart et al. (2008)
3 more