Research workbench
Structure of hIAPP-TF-type3
Analyse Structure of hIAPP-TF-type3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7YL7
- Type
- protein
- Length
- 402 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.3
- Molecule
- Islet amyloid polypeptide
- UniProt
- P10997
- Pockets
- 10 · best druggability 0.52
Structure
electron microscopy · resolution 3.3 · 2 distinct chains · 0% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F, A, B, J, E, I | Islet amyloid polypeptide | protein | 37 | 0% helix, 32% strand | P10997 |
| K, C, G, L, D, H | Islet amyloid polypeptide | protein | 30 | 0% helix, 57% strand | P10997 |
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 162 | 0.52 | 0.79 | 19 | empty |
| 2 | 161 | 0.51 | 0.78 | 20 | empty |
| 3 | 66 | 0.41 | 0.80 | 15 | empty |
| 4 | 99 | 0.38 | 0.76 | 22 | empty |
| 5 | 65 | 0.36 | 0.78 | 15 | empty |
Interfaces
35 interfaces between chains.
- F–A · 1509 Ų buried · 47 hydrogen bonds · protein-protein
- F–B · 1503 Ų buried · 47 hydrogen bonds · protein-protein
- J–E · 1502 Ų buried · 45 hydrogen bonds · protein-protein
- J–I · 1495 Ų buried · 44 hydrogen bonds · protein-protein
- D–H · 1253 Ų buried · 41 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified, 6 disulfide (nonstandard, disulfide).
Compared structures
- P10997 · AlphaFold monomer V2.0 prediction for islet amyloid polypeptide (P10997) · a predicted model of the same protein · chain A against A, TM-score 0.31
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 P10997
- Elsewhere: RCSB PDB 7YL7 · PDBe 7YL7 · UniProt P10997
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.