› 3wjy

X-ray diffraction
1.72Å resolution

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

Released:
DOI: 10.2210/pdb3wjy/pdb
PDB 3wjy coloured by chain and viewed from the front.
PDB 3wjy coloured by chain and viewed from the side.
PDB 3wjy coloured by chain and viewed from the top.
Source organism: Methanothermobacter thermautotrophicus str. Delta H
Primary publication:
Substrate distortion contributes to the catalysis of orotidine 5'-monophosphate decarboxylase.
Fujihashi M, Ishida T, Kuroda S, Kotra LP, Pai EF, Miki K
J. Am. Chem. Soc. 135 17432-43 (2013)
PMID: 24151964

Function and Biology Details

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

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:
Ligand NUP 1 x NUP
Ligand GOL 1 x GOL
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

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Citations

4 review citations

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