Research workbench
Cryo-EM structure of rtx-bound full-length TRPV1 in O1 state
Analyse Cryo-EM structure of rtx-bound full-length TRPV1 in O1 state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L2L
- Type
- protein
- Length
- 1,716 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transient receptor potential cation channel subfamily V member 1
- UniProt
- O35433
- Ligands
- 6EU
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 1 distinct chain · 63% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, B | Transient receptor potential cation channel subfamily V member 1 | protein | 429 | 63% helix, 3% strand | O35433 |
Ligands and binding sites
- 6EU · resiniferatoxin · ligand · 4 copies · chains A, D, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 397 | 0.85 | 0.93 | 28 | empty |
| 2 | 247 | 0.77 | 0.91 | 34 | empty |
| 3 | 354 | 0.73 | 0.84 | 41 | empty |
| 4 | 124 | 0.72 | 0.92 | 23 | empty |
| 5 | 465 | 0.71 | 0.81 | 46 | empty |
Interfaces
6 interfaces between chains.
- A–D · 2209 Ų buried · 10 hydrogen bonds · protein-protein
- C–B · 2163 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 2159 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 2148 Ų buried · 8 hydrogen bonds · protein-protein
- D–B · 28 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7L2L · Cryo-EM structure of RTX-bound full-length TRPV1 in O1 state · the same entry in another collection · chain A against A, TM-score 1.00
- O35433 · 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 O35433
- Elsewhere: RCSB PDB 7L2L · PDBe 7L2L · UniProt O35433
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