Structure analysis

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

X-ray diffraction
2.66Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero trimer (preferred)
Entry contents: 3 distinct polypeptide molecules

Assemblies

Assembly 1
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Multimeric state: hetero trimer
Accessible surface area: 17500 Å2
Buried surface area: 7300 Å2
Dissociation area: 1,300 Å2
Dissociation energy (ΔGdiss): 22 kcal/mol
Dissociation entropy (TΔSdiss): 9 kcal/mol
Interface energy (ΔGint): -47 kcal/mol
Symmetry number: 1
Assembly 2 (preferred)
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Multimeric state: hetero trimer
Accessible surface area: 17500 Å2
Buried surface area: 7900 Å2
Dissociation area: 1,300 Å2
Dissociation energy (ΔGdiss): 20 kcal/mol
Dissociation entropy (TΔSdiss): 9 kcal/mol
Interface energy (ΔGint): -46 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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