Research workbench
Three-protofilament amyloid structure of S20G variant of human amylin (iapp - islet amyloid polypeptide)
Analyse Three-protofilament amyloid structure of S20G variant of human amylin (iapp… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZRR
- Type
- protein
- Length
- 414 residues
- Chains
- 18
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Islet amyloid polypeptide
- UniProt
- P10997
- Pockets
- 3 · best druggability 0.72
Structure
electron microscopy · 1 distinct chain · 0% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R | Islet amyloid polypeptide | protein | 23 | 0% helix, 30% strand | P10997 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 206 | 0.72 | 0.89 | 45 | empty |
| 2 | 190 | 0.72 | 0.89 | 46 | empty |
| 3 | 67 | 0.62 | 0.91 | 30 | empty |
Interfaces
58 interfaces between chains.
- I–L · 899 Ų buried · 18 hydrogen bonds · protein-protein
- L–O · 899 Ų buried · 18 hydrogen bonds · protein-protein
- C–F · 894 Ų buried · 17 hydrogen bonds · protein-protein
- O–R · 892 Ų buried · 16 hydrogen bonds · protein-protein
- F–I · 890 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (nonstandard).
Compared structures
- 6ZRR · three-protofilament amyloid structure of S20G variant of human amylin (IAPP - Islet… · the same entry in another collection · chain R against R, 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 P10997
- Elsewhere: RCSB PDB 6ZRR · PDBe 6ZRR · UniProt P10997
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.