Structure analysis

Structure of the HCV1-C1 Antibody-Antigen Complex

X-ray diffraction
2.262Å 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: 20526.04 Å2
Buried surface area: 5481.73 Å2
Dissociation area: 634.07 Å2
Dissociation energy (ΔGdiss): 6.89 kcal/mol
Dissociation entropy (TΔSdiss): 8.15 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-210920
Assembly 2 (preferred)
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Multimeric state: hetero trimer
Accessible surface area: 20699.96 Å2
Buried surface area: 5153.94 Å2
Dissociation area: 608.59 Å2
Dissociation energy (ΔGdiss): 3.37 kcal/mol
Dissociation entropy (TΔSdiss): 8.14 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-210920
Assembly 3
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Multimeric state: hetero trimer
Accessible surface area: 20420.46 Å2
Buried surface area: 5824.9 Å2
Dissociation area: 644.27 Å2
Dissociation energy (ΔGdiss): 8.88 kcal/mol
Dissociation entropy (TΔSdiss): 8.16 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-210920
Assembly 4
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Multimeric state: hetero trimer
Accessible surface area: 20582.26 Å2
Buried surface area: 5340.29 Å2
Dissociation area: 602.59 Å2
Dissociation energy (ΔGdiss): 2.79 kcal/mol
Dissociation entropy (TΔSdiss): 8.14 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-210920

Macromolecules

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Chains: A, B, C, D
Length: 15 amino acids
Theoretical weight: 1.73 KDa
UniProt:
  • Canonical: P26663 (Residues: 412-423; Coverage: 0%)

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