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Desheptapeptide (B24-B30) insulin

Analyse Desheptapeptide (B24-B30) insulin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1DEI
Type
protein
Length
88 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Insulin
UniProt
P01315

Structure

x-ray diffraction · 2 distinct chains · 55% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CInsulinprotein2162% helix, 0% strandP01315
B, DInsulinprotein2348% helix, 0% strandP01315

Interfaces

6 interfaces between chains.

  • B–D · 570 Ų buried · 4 hydrogen bonds · protein-protein
  • C–D · 459 Ų buried · 4 hydrogen bonds · protein-protein
  • A–B · 447 Ų buried · 3 hydrogen bonds · protein-protein
  • B–C · 229 Ų buried · 3 hydrogen bonds · protein-protein
  • A–D · 218 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 1DEI · Desheptapeptide (B24-B30) insulin · the same entry in another collection · chain A against A, TM-score 1.00
  • P01315 · AlphaFold monomer V2.0 prediction for insulin (P01315) · a predicted model of the same protein · chain B against A, TM-score 0.42

Analyse

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