Research workbench
Cryo-EM structure of full-length TRPV1 at PH6C state
Analyse Cryo-EM structure of full-length TRPV1 at PH6C state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L2J
- Type
- protein
- Length
- 2,116 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
- XJ7
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 1 distinct chain · 57% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transient receptor potential cation channel subfamily V member 1 | protein | 529 | 57% helix, 4% strand | O35433 |
Ligands and binding sites
- XJ7 · (2S)-1-(butanoyloxy)-3-{[(R)-hydroxy{[(1r,2r,3s,4s,5r, 6S)-2,3,4,5,6-pentahydroxycyclohexyl]oxy}phosphoryl]oxy}propan-2-yl tridecanoate · ligand · 4 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 274 | 0.84 | 0.96 | 33 | empty |
| 2 | 1035 | 0.82 | 0.82 | 81 | XJ7 |
| 3 | 1164 | 0.81 | 0.82 | 101 | XJ7 |
| 4 | 1017 | 0.81 | 0.82 | 73 | XJ7 |
| 5 | 1011 | 0.81 | 0.82 | 75 | XJ7 |
Interfaces
6 interfaces between chains.
- A–D · 2496 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 2468 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 2456 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 2414 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 25 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 7L2J · PDBe 7L2J · UniProt O35433
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