Structure analysis

Crystal structure of human DNPH1 bound to hmdUMP

X-ray diffraction
1.78Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: homo dimer
Accessible surface area: 11548.78 Å2
Buried surface area: 5335.27 Å2
Dissociation area: 1,774.88 Å2
Dissociation energy (ΔGdiss): 18.03 kcal/mol
Dissociation entropy (TΔSdiss): 12.22 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-129016
Assembly 2 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 11562.25 Å2
Buried surface area: 4788.71 Å2
Dissociation area: 1,667.01 Å2
Dissociation energy (ΔGdiss): 24.23 kcal/mol
Dissociation entropy (TΔSdiss): 12.17 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-129016
Assembly 3
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Multimeric state: homo dimer
Accessible surface area: 11006.65 Å2
Buried surface area: 4489.57 Å2
Dissociation area: 1,514.21 Å2
Dissociation energy (ΔGdiss): 23.62 kcal/mol
Dissociation entropy (TΔSdiss): 11.98 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-129016

Macromolecules

Chains: A, B, C, D, E, F
Length: 147 amino acids
Theoretical weight: 16.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43598 (Residues: 19-162; Coverage: 83%)
Gene names: C6orf108, DNPH1, RCL
Pfam: Nucleoside 2-deoxyribosyltransferase

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