Structure analysis

Crystal Structure of human O-GlcNAc Transferase bound to a peptide from HCF-1 pro-repeat2(1-26) and UDP-GlcNAc

X-ray diffraction
2.55Å resolution
Source organism: Homo sapiens
Assembly composition:
Non-polymer only dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: Non-polymer only dimer
Accessible surface area: 27400 Å2
Buried surface area: 3800 Å2
Dissociation area: 1,400 Å2
Dissociation energy (ΔGdiss): 8 kcal/mol
Dissociation entropy (TΔSdiss): 10 kcal/mol
Interface energy (ΔGint): -12 kcal/mol
Symmetry number: 1

Macromolecules

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Chain: B
Length: 26 amino acids
Theoretical weight: 2.69 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P51610 (Residues: 1072-1097; Coverage: 1%)
Gene names: HCF1, HCFC1, HFC1

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