Research workbench
Structure and dynamics of des-pentapeptide-insulin in solution: the molten-globule hypothesis.
Analyse Structure and dynamics of des-pentapeptide-insulin in solution: the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HIS
- Type
- protein
- Length
- 46 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin
- UniProt
- P01308
Structure
solution nmr · 2 distinct chains · 33% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin | protein | 21 | 19% helix, 0% strand | P01308 |
| B | Insulin | protein | 25 | 44% helix, 0% strand | P01308 |
Interfaces
1 interface between chains.
- A–B · 662 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1HIS · Structure and dynamics of des-pentapeptide-insulin in solution: the molten-globule… · 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 P01308
- Elsewhere: RCSB PDB 1HIS · PDBe 1HIS · UniProt P01308
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