› 1dv7

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF OROTIDINE MONOPHOSPHATE DECARBOXYLASE

Released:
DOI: 10.2210/pdb1dv7/pdb
PDB entry 1dv7 coloured by chain, front view.
PDB entry 1dv7 coloured by chain, side view.
PDB entry 1dv7 coloured by chain, top view.
Source organism: Methanothermobacter thermautotrophicus
Primary publication:
Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase.
Wu N, Mo Y, Gao J, Pai EF
Proc Natl Acad Sci U S A 97 2017-22 (2000)
PMID: 10681441

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 Chain: A
Molecule details ›
Chain: A
Length: 227 amino acids
Theoretical weight: 24.75 KDa
Source organism: Methanothermobacter thermautotrophicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O26232 (Residues: 2-228; Coverage: 100%)
Gene names: MTH_129, 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: APS
Spacegroup: P41212
Unit cell:
a: 56.858Å b: 56.858Å c: 124.476Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.222
Expression system: Escherichia coli

Quick links

Citations

25 review citations

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

7 mentions without citation

Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase.
Wu et al. (2000)
6 more