3bgj

X-ray diffraction
2Å resolution

Crystal Structure of Human Orotidine 5'-monophosphate Decarboxylase Covalently Modified by 6-iodo-UMP

Released:
Source organism: Homo sapiens
Entry authors: Liu Y, Tang HL, Bello AM, Devalla S, Kotra LP, Pai EF

Function and Biology Details

Reactions catalysed:
Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate
Orotidine 5'-phosphate = UMP + CO(2)
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-145693 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uridine 5'-monophosphate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 291 amino acids
Theoretical weight: 31.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11172 (Residues: 190-480; Coverage: 61%)
Gene names: OK/SW-cl.21, UMPS
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: P21
Unit cell:
a: 69.803Å b: 61.821Å c: 70.881Å
α: 90° β: 111.66° γ: 90°
R-values:
R R work R free
0.173 0.172 0.209
Expression system: Escherichia coli