Research workbench
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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Insulin | protein | 21 | 62% helix, 0% strand | P01315 |
| B, D | Insulin | protein | 23 | 48% helix, 0% strand | P01315 |
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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P01315
- Elsewhere: RCSB PDB 1DEI · PDBe 1DEI · UniProt P01315
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