Research workbench
Cryo-EM structure of human islet amyloid polypeptide (hiapp, or amylin) fibrils seeded by patient extracted fibrils, polymorph 4
Analyse Cryo-EM structure of human islet amyloid polypeptide (hiapp, or amylin) fibrils… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7M65
- Type
- protein
- Length
- 275 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P10997
- Ligands
- NH2
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I | — | protein | 32 | — | P10997 |
| B, D, F, H, J | — | protein | 23 | — | P10997 |
Ligands and binding sites
- NH2 · Amino group · ion · 5 copies · chains A, J, C, F, E, H, B, G, I
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7M65 · Cryo-EM structure of human islet amyloid polypeptide (hIAPP, or amylin) fibrils seeded by… · the same entry in another collection · chain I against I, 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 0.22
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 7M65 · PDBe 7M65 · UniProt P10997
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