Research workbench
Structure of apo-HSTRPM2 channel
Analyse Structure of apo-HSTRPM2 channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VQ1
- Type
- protein
- Length
- 5,208 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 · 48% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transient receptor potential cation channel subfamily M member 2 | protein | 1302 | 48% helix, 9% 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 | 953 | 0.88 | 0.89 | 109 | empty |
| 2 | 398 | 0.80 | 0.88 | 51 | empty |
| 3 | 1008 | 0.80 | 0.81 | 76 | empty |
| 4 | 962 | 0.80 | 0.81 | 76 | empty |
| 5 | 374 | 0.79 | 0.88 | 41 | empty |
Interfaces
4 interfaces between chains.
- C–D · 2221 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 2206 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 2199 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 2170 Ų buried · 7 hydrogen bonds · protein-protein
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 7VQ1 · PDBe 7VQ1 · UniProt O94759
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