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Structure of TRPV3 in complex with osthole

Analyse Structure of TRPV3 in complex with osthole in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7RAS
Type: protein
Length: 2,440 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transient receptor potential cation channel subfamily V member 3
UniProt: Q8K424
Ligands: A0O
Pockets: 20 · best druggability 0.70

Structure

electron microscopy · 1 distinct chain · 58% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Transient receptor potential cation channel subfamily V member 3	protein	610	58% helix, 5% strand	Q8K424

Ligands and binding sites

A0O · 7-methoxy-8-(3-methylbut-2-enyl)chromen-2-one · ligand · 8 copies · chains A, B, C, D

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	606	0.70	0.78	78	empty
2	546	0.69	0.78	70	empty
3	411	0.68	0.80	36	A0O
4	82	0.67	0.93	18	empty
5	477	0.67	0.78	50	empty

Interfaces

4 interfaces between chains.

A–B · 2392 Å² buried · 12 hydrogen bonds · protein-protein
B–C · 2391 Å² buried · 12 hydrogen bonds · protein-protein
A–D · 2390 Å² buried · 12 hydrogen bonds · protein-protein
C–D · 2388 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

7RAS · Structure of TRPV3 in complex with osthole · the same entry in another collection · chain A against A, TM-score 1.00
Q8K424 · AlphaFold monomer V2.0 prediction for transient receptor potential cation channel… · a predicted model of the same protein · chain A against A, TM-score 0.91

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 Q8K424
Elsewhere: RCSB PDB 7RAS · PDBe 7RAS · UniProt Q8K424

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