Structure analysis

Crystal structure of MN human arg-insulin

X-ray diffraction
2.25Å resolution
Source organism: Homo sapiens
Assembly composition:
Non-polymer only dodecamer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: Non-polymer only dodecamer
Accessible surface area: 14600 Å2
Buried surface area: 17400 Å2
Dissociation area: 100 Å2
Dissociation energy (ΔGdiss): 8 kcal/mol
Dissociation entropy (TΔSdiss): 1 kcal/mol
Interface energy (ΔGint): -172 kcal/mol
Symmetry number: 3

Macromolecules

Chains: A, C
Length: 22 amino acids
Theoretical weight: 2.54 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P01308 (Residues: 89-110; Coverage: 26%)
Gene name: INS
InterPro:

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Chains: B, D
Length: 30 amino acids
Theoretical weight: 3.43 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P01308 (Residues: 25-54; Coverage: 35%)
Gene name: INS
InterPro:
SCOP: Isolated insulin B-chain

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