3wjy

X-ray diffraction
1.72Å resolution

Orotidine 5'-monophosphate decarboxylase K72A mutant from M. thermoautotrophicus complexed with 6-amino-UMP

Released:

Function and Biology Details

Reaction catalysed:
Orotidine 5'-phosphate = UMP + CO(2)
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Orotidine 5'-phosphate decarboxylase Chain: A
Molecule details ›
Chain: A
Length: 252 amino acids
Theoretical weight: 27.32 KDa
Source organism: Methanothermobacter thermautotrophicus str. Delta H
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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: C2221
Unit cell:
a: 58.118Å b: 103.527Å c: 74.046Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.149 0.181
Expression system: Escherichia coli