Research workbench
Cryo-EM study of a channel
Analyse Cryo-EM study of a channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JAC
- Type
- protein
- Length
- 2,754 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 0.76
Structure
electron microscopy · 1 distinct chain · 69% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Piezo-type mechanosensitive ion channel component 1 | protein | 918 | 69% helix, 9% strand | E2JF22 |
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 341 | 0.76 | 0.88 | 50 | empty |
| 2 | 1155 | 0.74 | 0.77 | 124 | empty |
| 3 | 902 | 0.73 | 0.77 | 117 | empty |
| 4 | 881 | 0.72 | 0.77 | 111 | empty |
| 5 | 542 | 0.65 | 0.77 | 63 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1066 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 967 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 891 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
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 3JAC · PDBe 3JAC · UniProt E2JF22
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