PDBe 4hkp

X-ray diffraction
1.75Å resolution

Crystal structure of human orotidine 5'-monophosphate decarboxylase complexed with CMP-N3-oxide

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uridine 5'-monophosphate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 312 amino acids
Theoretical weight: 34.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11172 (Residues: 190-480; Coverage: 61%)
  • Best match: P11172-2 (Residues: 12-302)
Gene names: OK/SW-cl.21, UMPS
Sequence domains: Orotidine 5'-phosphate decarboxylase / HUMPS family
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P21
Unit cell:
a: 69.29Å b: 61.775Å c: 70.523Å
α: 90° β: 112.9° γ: 90°
R-values:
R R work R free
0.161 0.161 0.186
Expression system: Escherichia coli