Structure analysis

Crystal Structure of HLA-DR1 with CLIP106-120, canonical peptide orientation

X-ray diffraction
2.72Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero trimer (preferred)
Entry contents: 3 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero trimer
Accessible surface area: 17800 Å2
Buried surface area: 7300 Å2
Dissociation area: 1,200 Å2
Dissociation energy (ΔGdiss): 19 kcal/mol
Dissociation entropy (TΔSdiss): 9 kcal/mol
Interface energy (ΔGint): -48 kcal/mol
Symmetry number: 1
Assembly 2
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Multimeric state: hetero trimer
Accessible surface area: 17900 Å2
Buried surface area: 7400 Å2
Dissociation area: 1,200 Å2
Dissociation energy (ΔGdiss): 18 kcal/mol
Dissociation entropy (TΔSdiss): 9 kcal/mol
Interface energy (ΔGint): -49 kcal/mol
Symmetry number: 1

Macromolecules

Chains: C, F
Length: 15 amino acids
Theoretical weight: 1.73 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P04233 (Residues: 106-120; Coverage: 5%)
Gene names: CD74, DHLAG

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