MolNFT v1 · #180529 · protein

Cryo-EM structure of rtx-bound full-length TRPV1 in O1 state

7L2L · Transient receptor potential cation channel subfamily V…: “Cryo-EM structure of rtx-bound full-length TRPV1 in O1 state”. Electron microscopy, 1 ligand (6EU), 20 pockets (best druggability 0.85). MolNFT v1 #180529 on GenesisL1: 3D…

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.

Pocket	Volume (Å³)	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 Å² buried · 10 hydrogen bonds · protein-protein
C–B · 2163 Å² buried · 10 hydrogen bonds · protein-protein
C–D · 2159 Å² buried · 10 hydrogen bonds · protein-protein
A–B · 2148 Å² buried · 8 hydrogen bonds · protein-protein
D–B · 28 Å² 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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