MolNFT v1 · #181790 · protein
Cryo-EM structure of human islet amyloid polypeptide (hiapp, or amylin) fibrils seeded by patient extracted fibrils, polymorph 3
7M64: “Cryo-EM structure of human islet amyloid polypeptide (hiapp, or amylin) fibrils seeded by patient extracted…”. Electron microscopy, 1 ligand (NH2), 1 pocket (best druggability 0.45). MolNFT v1 #181790 on GenesisL1: 3D structure…
- PDB
- 7M64
- Type
- protein
- Length
- 250 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Islet amyloid polypeptide
- UniProt
- P10997
- Ligands
- NH2
- Pockets
- 1 · best druggability 0.45
Structure
electron microscopy · 1 distinct chain · 0% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Islet amyloid polypeptide | protein | 25 | 0% helix, 36% strand | P10997 |
Ligands and binding sites
- NH2 · Amino group · ion · 10 copies · chains A, C, D, B, F, E, H, G, J, I
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.45 | 0.84 | 28 | empty |
Interfaces
30 interfaces between chains.
- D–H · 1004 Ų buried · 26 hydrogen bonds · protein-protein
- A–D · 1003 Ų buried · 26 hydrogen bonds · protein-protein
- B–F · 1001 Ų buried · 26 hydrogen bonds · protein-protein
- B–C · 999 Ų buried · 26 hydrogen bonds · protein-protein
- F–J · 999 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 7M64 · Cryo-EM structure of human islet amyloid polypeptide (hIAPP, or amylin) fibrils seeded by… · the same entry in another collection · chain J against J, TM-score 1.00
- P10997 · AlphaFold monomer V2.0 prediction for islet amyloid polypeptide (P10997) · a predicted model of the same protein · chain A against A, TM-score 0.17
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 7M64 · PDBe 7M64 · UniProt P10997
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