Research workbench
Cryo-EM structure of full-length TRPV1 at PH6A state
Analyse Cryo-EM structure of full-length TRPV1 at PH6A state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L2I
- Type
- protein
- Length
- 2,124 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
- XJA
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 1 distinct chain · 58% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, B | Transient receptor potential cation channel subfamily V member 1 | protein | 531 | 58% helix, 4% strand | O35433 |
Ligands and binding sites
- XJA · (2S)-1-(butanoyloxy)-3-{[(R)-hydroxy{[(1s,2r,3r,4r,5r, 6S)-2,3,4,5,6-pentahydroxycyclohexyl]oxy}phosphoryl]oxy}propan-2-yl tridecanoate · 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, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 273 | 0.84 | 0.96 | 31 | empty |
| 2 | 1013 | 0.82 | 0.83 | 87 | XJA |
| 3 | 1028 | 0.80 | 0.81 | 76 | XJA |
| 4 | 1194 | 0.80 | 0.81 | 96 | XJA |
| 5 | 1146 | 0.79 | 0.81 | 88 | XJA |
Interfaces
6 interfaces between chains.
- A–B · 2638 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 2601 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 2586 Ų buried · 10 hydrogen bonds · protein-protein
- C–B · 2566 Ų buried · 8 hydrogen bonds · protein-protein
- D–B · 32 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 7L2I · PDBe 7L2I · UniProt O35433
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