Research workbench
Cryo-EM structure of rtx-bound full-length TRPV1 in C2 state
Analyse Cryo-EM structure of rtx-bound full-length TRPV1 in C2 state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MZ5
- Type
- protein
- Length
- 1,724 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, NA
- Pockets
- 20 · best druggability 0.89
Structure
electron microscopy · 1 distinct chain · 62% 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 | 431 | 62% helix, 4% strand | O35433 |
Ligands and binding sites
- 6EU · resiniferatoxin · ligand · 4 copies · chains A, D, C, B
- NA · Sodium ion · metal · 3 copies · chains A, C, D, 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 | 1131 | 0.89 | 0.89 | 103 | NA |
| 2 | 561 | 0.73 | 0.81 | 59 | empty |
| 3 | 472 | 0.71 | 0.81 | 53 | empty |
| 4 | 504 | 0.71 | 0.80 | 54 | empty |
| 5 | 440 | 0.70 | 0.81 | 46 | empty |
Interfaces
6 interfaces between chains.
- A–D · 2139 Ų buried · 10 hydrogen bonds · protein-protein
- C–B · 2129 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 2114 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 2091 Ų buried · 9 hydrogen bonds · protein-protein
- D–B · 32 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7MZ5 · Cryo-EM structure of RTX-bound full-length TRPV1 in C2 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 7MZ5 · PDBe 7MZ5 · UniProt O35433
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