Research workbench

Structure of MTRPV2_E2

Analyse Structure of MTRPV2_E2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7XEU
Type: protein
Length: 2,456 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transient receptor potential cation channel subfamily V member 2
UniProt: Q9WTR1
Ligands: CLR
Pockets: 20 · best druggability 0.83

Structure

electron microscopy · 1 distinct chain · 53% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Transient receptor potential cation channel subfamily V member 2	protein	614	53% helix, 4% strand	Q9WTR1

Ligands and binding sites

CLR · Cholesterol · ligand · 4 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, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	459	0.83	0.90	41	empty
2	209	0.82	0.96	33	empty
3	438	0.82	0.90	38	empty
4	421	0.81	0.89	37	empty
5	443	0.81	0.88	41	empty

Interfaces

6 interfaces between chains.

A–D · 2769 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 2759 Å² buried · 8 hydrogen bonds · protein-protein
A–B · 2742 Å² buried · 6 hydrogen bonds · protein-protein
C–D · 2733 Å² buried · 6 hydrogen bonds · protein-protein
A–C · 41 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7XEU · Structure of mTRPV2_E2 · the same entry in another collection · chain A against A, TM-score 1.00
Q9WTR1 · AlphaFold monomer V2.0 prediction for transient receptor potential cation channel… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q9WTR1
Elsewhere: RCSB PDB 7XEU · PDBe 7XEU · UniProt Q9WTR1

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