Research workbench
Structure of the mechanosensitive PIEZO1 channel
Analyse Structure of the mechanosensitive PIEZO1 channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Z10
- Type
- protein
- Length
- 3,912 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Piezo-type mechanosensitive ion channel component 1
- UniProt
- E2JF22
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 58% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Piezo-type mechanosensitive ion channel component 1 | protein | 1304 | 58% helix, 6% strand | E2JF22 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 411 | 0.83 | 0.91 | 51 | empty |
| 2 | 945 | 0.82 | 0.84 | 107 | empty |
| 3 | 1197 | 0.81 | 0.82 | 106 | empty |
| 4 | 884 | 0.80 | 0.82 | 68 | empty |
| 5 | 925 | 0.78 | 0.79 | 92 | empty |
Interfaces
3 interfaces between chains.
- A–C · 3454 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 3451 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 3451 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 5Z10 · Structure of the mechanosensitive Piezo1 channel · the same entry in another collection · chain A against A, TM-score 1.00
- E2JF22 · AlphaFold monomer V2.0 prediction for piezo-type mechanosensitive ion channel component 1… · a predicted model of the same protein · chain A against A, TM-score 0.79
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 E2JF22
- Elsewhere: RCSB PDB 5Z10 · PDBe 5Z10 · UniProt E2JF22
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