Structure analysis

NMR structure of human insulin mutant GLY-B8-D-SER, HIS-B10-ASP PRO-B28-LYS, LYS-B29-PRO, 20 structures

Solution NMR
Source organism: Homo sapiens
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 3700 Å2
Buried surface area: 1400 Å2
Dissociation area: 700 Å2
Dissociation energy (ΔGdiss): 20 kcal/mol
Dissociation entropy (TΔSdiss): 8 kcal/mol
Interface energy (ΔGint): -19 kcal/mol
Symmetry number: 1

Macromolecules

Chain: A
Length: 21 amino acids
Theoretical weight: 2.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01308 (Residues: 90-110; Coverage: 24%)
Gene name: INS
InterPro:

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Chain: B
Length: 30 amino acids
Theoretical weight: 3.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01308 (Residues: 25-54; Coverage: 35%)
Gene name: INS
InterPro:

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