2jgy

X-ray diffraction
1.95Å resolution

The crystal structure of human orotidine-5'-decarboxylase domain of human uridine monophosphate synthetase (UMPS)

Released:
Source organism: Homo sapiens
Entry authors: Moche M, Ogg D, Arrowsmith C, Berglund H, Busam R, Collins R, Dahlgren LG, Edwards A, Ericsson UB, Flodin S, Flores A, Graslund S, Hammarstrom M, Hallberg BM, Holmberg-Schiavone L, Johansson I, Karlberg T, Kosinska U, Kotenyova T, Lehtio L, Nilsson ME, Nyman T, Persson C, Sagemark J, Stenmark P, Sundstrom M, Uppenberg J, Upsten M, Thorsell AG, van den Berg S, Weigelt J, Nordlund P, Structural Genomics Consortium (SGC)

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: 279 amino acids
Theoretical weight: 30.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P11172 (Residues: 224-479; Coverage: 53%)
Gene names: OK/SW-cl.21, UMPS
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: MAX II BEAMLINE I911-2
Spacegroup: P212121
Unit cell:
a: 59.83Å b: 77.83Å c: 152.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.197
Expression system: Escherichia coli BL21(DE3)