Research workbench
Cryo-EM structure of full-length TRPV1 at PH6B state
Analyse Cryo-EM structure of full-length TRPV1 at PH6B state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L2K
- Type
- protein
- Length
- 1,976 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
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 1 distinct chain · 61% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, B | Transient receptor potential cation channel subfamily V member 1 | protein | 494 | 61% helix, 2% strand | O35433 |
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 | 293 | 0.85 | 0.95 | 35 | empty |
| 2 | 1048 | 0.82 | 0.82 | 101 | empty |
| 3 | 1061 | 0.81 | 0.82 | 96 | empty |
| 4 | 1034 | 0.81 | 0.82 | 83 | empty |
| 5 | 609 | 0.77 | 0.83 | 54 | empty |
Interfaces
6 interfaces between chains.
- A–D · 2148 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 2138 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 2128 Ų buried · 4 hydrogen bonds · protein-protein
- C–B · 2056 Ų buried · 5 hydrogen bonds · protein-protein
- D–B · 33 Ų buried · 0 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 O35433
- Elsewhere: RCSB PDB 7L2K · PDBe 7L2K · UniProt O35433
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