Research workbench
Structure of TRPM2 ion channel receptor by single particle electron cryo-microscopy, apo state
Analyse Structure of TRPM2 ion channel receptor by single particle electron… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DRK
- Type
- protein
- Length
- 5,060 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transient receptor potential cation channel, subfamily M, member 2
- UniProt
- A0A0R4IN04
- Pockets
- 20 · best druggability 0.79
Structure
electron microscopy · 1 distinct chain · 49% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, B, D | Transient receptor potential cation channel, subfamily M, member 2 | protein | 1265 | 49% helix, 9% strand | A0A0R4IN04 |
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 | 871 | 0.79 | 0.82 | 95 | empty |
| 2 | 919 | 0.79 | 0.81 | 86 | empty |
| 3 | 1187 | 0.78 | 0.80 | 111 | empty |
| 4 | 872 | 0.78 | 0.80 | 81 | empty |
| 5 | 1173 | 0.77 | 0.79 | 116 | empty |
Interfaces
6 interfaces between chains.
- A–D · 2164 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 2137 Ų buried · 2 hydrogen bonds · protein-protein
- C–B · 2131 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 2130 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 16 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6DRK · Structure of TRPM2 ion channel receptor by single particle electron cryo-microscopy, Apo… · 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
- Every structure of UniProt A0A0R4IN04
- Elsewhere: RCSB PDB 6DRK · PDBe 6DRK · UniProt A0A0R4IN04
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