Research workbench
Human TRPM2 ion channel in apo state
Analyse Human TRPM2 ion channel in apo state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MIX
- Type
- protein
- Length
- 5,348 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
- O94759
- Pockets
- 20 · best druggability 0.88
Structure
electron microscopy · 1 distinct chain · 41% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transient receptor potential cation channel subfamily M member 2 | protein | 1337 | 41% helix, 8% strand | O94759 |
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 | 1107 | 0.88 | 0.89 | 132 | empty |
| 2 | 970 | 0.83 | 0.84 | 96 | empty |
| 3 | 777 | 0.83 | 0.85 | 85 | empty |
| 4 | 470 | 0.82 | 0.89 | 63 | empty |
| 5 | 808 | 0.82 | 0.85 | 83 | empty |
Interfaces
6 interfaces between chains.
- A–D · 3880 Ų buried · 36 hydrogen bonds · protein-protein
- C–D · 3858 Ų buried · 41 hydrogen bonds · protein-protein
- A–B · 3841 Ų buried · 40 hydrogen bonds · protein-protein
- B–C · 3807 Ų buried · 45 hydrogen bonds · protein-protein
- B–D · 27 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 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 O94759
- Elsewhere: RCSB PDB 6MIX · PDBe 6MIX · UniProt O94759
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