Research workbench
Cryo-EM structure of the mouse Piezo1 isoform Piezo1.1
Analyse Cryo-EM structure of the mouse Piezo1 isoform Piezo1.1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LQI
- Type
- protein
- Length
- 3,903 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 4.5
- Source
- Mus musculus
- Molecule
- Piezo-type mechanosensitive ion channel component 1
- UniProt
- E2JF22
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · resolution 4.5 · 1 distinct chain · 61% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Piezo-type mechanosensitive ion channel component 1 | protein | 1301 | 61% 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 | 889 | 0.83 | 0.85 | 81 | empty |
| 2 | 1070 | 0.83 | 0.84 | 139 | empty |
| 3 | 851 | 0.83 | 0.85 | 70 | empty |
| 4 | 1029 | 0.83 | 0.84 | 140 | empty |
| 5 | 918 | 0.82 | 0.85 | 129 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2698 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 2681 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 2673 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 6LQI · Cryo-EM structure of the mouse PIEZO1 isoform PIEZO1.1 · 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 0.78
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 6LQI · PDBe 6LQI · UniProt E2JF22
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