PDBe 1dbt

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH UMP

Released:
Source organism: Bacillus subtilis
Primary publication:
The crystal structure and mechanism of orotidine 5'-monophosphate decarboxylase.
Proc. Natl. Acad. Sci. U.S.A. 97 2005-10 (2000)
PMID: 10681442

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Orotidine 5'-phosphate decarboxylase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 239 amino acids
Theoretical weight: 26.02 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P25971 (Residues: 1-239; Coverage: 100%)
Gene names: BSU15550, pyrF
Sequence domains: Orotidine 5'-phosphate decarboxylase / HUMPS family
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21212
Unit cell:
a: 78.41Å b: 89.76Å c: 105.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 0.228
Expression system: Escherichia coli