Research workbench
Prion derived tetrapeptide stabilizes thermolabile insulin via conformational trapping
Analyse Prion derived tetrapeptide stabilizes thermolabile insulin via conformational… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ELJ
- Type
- protein
- Length
- 55 residues
- Chains
- 3
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin a chain; Insulin B chain; IS1
- UniProt
- P01317
Structure
solution nmr · 3 distinct chains · 45% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin a chain | protein | 21 | 48% helix, 10% strand | P01317 |
| B | Insulin B chain | protein | 30 | 50% helix, 7% strand | P01317 |
| C | IS1 | protein | 4 | 0% helix, 0% strand | — |
Interfaces
3 interfaces between chains.
- A–B · 924 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 312 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 61 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7ELJ · Prion Derived Tetrapeptide Stabilizes Thermolabile Insulin via Conformational Trapping · the same entry in another collection · chain A against A, TM-score 1.00
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 P01317
- Elsewhere: RCSB PDB 7ELJ · PDBe 7ELJ · UniProt P01317
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