Structure analysis

Crystal structure of human orotidine 5'-monophosphate decarboxylase complexed with CMP-N4-OH

X-ray diffraction
1.8Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 18230.57 Å2
Buried surface area: 4359.24 Å2
Dissociation area: 1,933 Å2
Dissociation energy (ΔGdiss): 28.78 kcal/mol
Dissociation entropy (TΔSdiss): 13.26 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-145693

Macromolecules

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%)
Gene names: OK/SW-cl.21, UMPS
Pfam: Orotidine 5'-phosphate decarboxylase / HUMPS family
InterPro:
CATH: Aldolase class I

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