Structure analysis

Ketopiperazine-Based Renin Inhibitors: Optimization of the "C" Ring

X-ray diffraction
2.1Å resolution
Source organism: Homo sapiens
Assemblies composition:
monomeric (preferred)
homo hexamer
homo trimer
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: monomeric

Binding statistics and energies are not available for this assembly
Assembly 2 (preferred)
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Multimeric state: monomeric
Accessible surface area: 14400 Å2
Buried surface area: 1100 Å2
Dissociation area: 550 Å2
Dissociation energy (ΔGdiss): -6 kcal/mol
Dissociation entropy (TΔSdiss): 6 kcal/mol
Interface energy (ΔGint): 0 kcal/mol
Symmetry number: 1
Assembly 3
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Multimeric state: homo hexamer
Accessible surface area: 73600 Å2
Buried surface area: 15900 Å2
Dissociation area: 6,200 Å2
Dissociation energy (ΔGdiss): 3 kcal/mol
Dissociation entropy (TΔSdiss): 71 kcal/mol
Interface energy (ΔGint): -59 kcal/mol
Symmetry number: 3
Assembly 4
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Multimeric state: homo trimer
Accessible surface area: 39500 Å2
Buried surface area: 7200 Å2
Dissociation area: 1,900 Å2
Dissociation energy (ΔGdiss): 2 kcal/mol
Dissociation entropy (TΔSdiss): 28 kcal/mol
Interface energy (ΔGint): -26 kcal/mol
Symmetry number: 3

Macromolecules

Chains: A, B
Length: 333 amino acids
Theoretical weight: 36.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00797 (Residues: 74-406; Coverage: 87%)
Gene name: REN
Pfam: Eukaryotic aspartyl protease
InterPro:
CATH: Acid Proteases

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