Structure analysis

Human insulin B26Asn mutant crystal structure

X-ray diffraction
1.81Å resolution
Source organism: Homo sapiens
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: 3900 Å2
Buried surface area: 1100 Å2
Dissociation area: 550 Å2
Dissociation energy (ΔGdiss): 17 kcal/mol
Dissociation entropy (TΔSdiss): 8 kcal/mol
Interface energy (ΔGint): -13 kcal/mol
Symmetry number: 1
Assembly 2 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 3900 Å2
Buried surface area: 1300 Å2
Dissociation area: 600 Å2
Dissociation energy (ΔGdiss): 16 kcal/mol
Dissociation entropy (TΔSdiss): 8 kcal/mol
Interface energy (ΔGint): -24 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, C
Length: 21 amino acids
Theoretical weight: 2.38 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P01308 (Residues: 90-110; Coverage: 24%)
Gene name: INS
InterPro:

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Chains: B, D
Length: 30 amino acids
Theoretical weight: 3.38 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P01308 (Residues: 25-54; Coverage: 35%)
Gene name: INS
InterPro:

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