2wns

X-ray diffraction
1.9Å resolution

Human Orotate phosphoribosyltransferase (OPRTase) domain of Uridine 5' -monophosphate synthase (UMPS) in complex with its substrate orotidine 5'-monophosphate (OMP)

Released:
Source organism: Homo sapiens
Entry authors: Moche M, Roos A, Arrowsmith CH, Berglund H, Bountra C, Collins R, Edwards AM, Flodin S, Flores A, Graslund S, Hammarstrom M, Johansson A, Johansson I, Karlberg T, Kotyenova T, Kotzch A, Nielsen TK, Nyman T, Persson C, Sagemark J, Schueler H, Schutz P, Siponen MI, Svensson L, Thorsell AG, Tresaugues L, VanDenBerg S, Weigelt J, Welin M, Wisniewska M, Nordlund P

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: 205 amino acids
Theoretical weight: 22.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P11172 (Residues: 7-203; Coverage: 41%)
Gene names: OK/SW-cl.21, UMPS
Sequence domains: Phosphoribosyl transferase domain
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 64.4Å b: 43.6Å c: 71Å
α: 90° β: 113.4° γ: 90°
R-values:
R R work R free
0.182 0.18 0.228
Expression system: Escherichia coli BL21(DE3)