Structure analysis

Structure of human insulin in presence of urea at pH 6.5

X-ray diffraction
2.05Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero dodecamer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1
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Multimeric state: hetero dodecamer
Accessible surface area: 12632.43 Å2
Buried surface area: 21067.34 Å2
Dissociation area: 4,325.87 Å2
Dissociation energy (ΔGdiss): 37.52 kcal/mol
Dissociation entropy (TΔSdiss): 12.75 kcal/mol
Symmetry number: 6
PDBe Complex ID: PDB-CPX-134235
Assembly 2
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Multimeric state: hetero dodecamer
Accessible surface area: 12504.22 Å2
Buried surface area: 20843.72 Å2
Dissociation area: 353.4 Å2
Dissociation energy (ΔGdiss): 86.14 kcal/mol
Dissociation entropy (TΔSdiss): 2.18 kcal/mol
Symmetry number: 6
PDBe Complex ID: PDB-CPX-134235
Assembly 3 (preferred)
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Multimeric state: hetero dodecamer
Accessible surface area: 12453.2 Å2
Buried surface area: 20505.11 Å2
Dissociation area: 353.61 Å2
Dissociation energy (ΔGdiss): 85.69 kcal/mol
Dissociation entropy (TΔSdiss): 2.12 kcal/mol
Symmetry number: 6
PDBe Complex ID: PDB-CPX-134235

Macromolecules

Chains: 1, 3, A, C, E, G, I, K, Q, S, U, X, a, c, e, g, i, k
Length: 21 amino acids
Theoretical weight: 2.38 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P01308 (Residues: 90-110; Coverage: 24%)
Gene name: INS
InterPro:
PDBe-KB: UniProt Coverage View: P01308  
1212468101214161820
 
5101520GIVEQCCTSICSLYQLENYCN
UniProt
P01308
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces

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Chains: 2, 4, B, D, F, H, J, L, R, T, V, Y, b, d, f, h, j, l
Length: 30 amino acids
Theoretical weight: 3.43 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P01308 (Residues: 25-54; Coverage: 35%)
Gene name: INS
Pfam: Insulin/IGF/Relaxin family
InterPro:
SCOP: Isolated insulin B-chain
PDBe-KB: UniProt Coverage View: P01308  
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