MolNFT v1 · #121004 · protein
Structure of the full-length TRPV2 channel by cryo-electron microscopy
5HI9 · Transient receptor potential cation channel subfamily V…: “Structure of the full-length TRPV2 channel by cryo-electron microscopy”. Electron microscopy, 20 pockets (best druggability 0.80). MolNFT v1 #121004 on GenesisL1: 3D…
- PDB
- 5HI9
- Type
- protein
- Length
- 2,408 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transient receptor potential cation channel subfamily V member 2
- UniProt
- Q9WUD2
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · 1 distinct chain · 51% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transient receptor potential cation channel subfamily V member 2 | protein | 602 | 51% helix, 3% strand | Q9WUD2 |
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 | 216 | 0.80 | 0.94 | 38 | empty |
| 2 | 206 | 0.80 | 0.93 | 37 | empty |
| 3 | 384 | 0.80 | 0.88 | 48 | empty |
| 4 | 569 | 0.79 | 0.85 | 72 | empty |
| 5 | 664 | 0.79 | 0.84 | 86 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2246 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 2237 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 2228 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 2217 Ų buried · 14 hydrogen bonds · protein-protein
- B–D · 20 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5HI9 · Structure of the full-length TRPV2 channel by cryo-electron microscopy · the same entry in another collection · chain A against A, TM-score 1.00
- Q9WUD2 · AlphaFold monomer V2.0 prediction for transient receptor potential cation channel… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q9WUD2
- Elsewhere: RCSB PDB 5HI9 · PDBe 5HI9 · UniProt Q9WUD2
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