Research workbench
Cryo-EM structure of the TRPM8 ion channel with low occupancy icilin, PI(4,5)P2, and calcium
Analyse Cryo-EM structure of the TRPM8 ion channel with low occupancy icilin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NR4
- Type
- protein
- Length
- 3,216 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 4.3
- Source
- Ficedula albicollis
- Molecule
- Transient receptor potential cation channel subfamily M member 8
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · resolution 4.3 · 1 distinct chain · 67% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transient receptor potential cation channel subfamily M member 8 | protein | 804 | 67% helix, 4% strand | — |
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 | 896 | 0.82 | 0.84 | 70 | empty |
| 2 | 1071 | 0.80 | 0.81 | 81 | empty |
| 3 | 1139 | 0.80 | 0.81 | 90 | empty |
| 4 | 1127 | 0.80 | 0.81 | 92 | empty |
| 5 | 892 | 0.74 | 0.78 | 96 | empty |
Interfaces
4 interfaces between chains.
- A–D · 2287 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 2281 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 2279 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 2277 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6NR4 · Cryo-EM structure of the TRPM8 ion channel with low occupancy icilin, PI(4,5)P2, and… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 6NR4 · PDBe 6NR4
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