Structure analysis

The structures of Ace2 in complex with bicyclic peptide inhibitor

X-ray diffraction
2.61Å resolution
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1
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Multimeric state: hetero dimer
Accessible surface area: 24958.89 Å2
Buried surface area: 2970.28 Å2
Dissociation area: 1,335.76 Å2
Dissociation energy (ΔGdiss): 17.76 kcal/mol
Dissociation entropy (TΔSdiss): 8.8 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-229375
Assembly 2 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 25006.57 Å2
Buried surface area: 2941.57 Å2
Dissociation area: 1,371.08 Å2
Dissociation energy (ΔGdiss): 18.19 kcal/mol
Dissociation entropy (TΔSdiss): 8.81 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-229375

Macromolecules

Chains: A, B
Length: 609 amino acids
Theoretical weight: 70.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BYF1 (Residues: 19-615; Coverage: 76%)
Gene names: ACE2, UNQ868/PRO1885
Pfam: Angiotensin-converting enzyme

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