2v30

X-ray diffraction
2Å resolution

Human orotidine 5'-phosphate decarboxylase domain of uridine monophospate synthetase (UMPS) in complex with its product UMP.

Released:
Source organism: Homo sapiens
Entry authors: Moche M, Ogg D, Arrowsmith C, Berglund H, Busam R, Collins R, Dahlgren LG, Edwards A, Flodin S, Flores A, Graslund S, Hammarstrom M, Hallberg BM, Holmberg-Schiavone L, Johansson I, Kallas A, Karlberg T, Kotenyova T, Lehtio L, Nyman T, Persson C, Sagemark J, Stenmark P, Sundstrom M, Thorsell AG, van den Berg S, Weigelt J, Welin M, 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

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 60.103Å b: 77.853Å c: 153.209Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.153 0.188
Expression system: Escherichia coli BL21(DE3)