MolNFT v1 · #190531 · protein

Structure of MTRPV2_Q525T

7XER · Transient receptor potential cation channel subfamily V…: “Structure of MTRPV2_Q525T”. Electron microscopy, 1 ligand (CLR), 20 pockets (best druggability 0.83). MolNFT v1 #190531 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 7XER
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 · 55% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Transient receptor potential cation channel subfamily V member 2	protein	614	55% helix, 5% 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, 16 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	300	0.83	0.94	30	empty
2	430	0.80	0.88	49	empty
3	429	0.79	0.87	40	empty
4	434	0.79	0.87	47	empty
5	436	0.78	0.86	42	empty

Interfaces

6 interfaces between chains.

C–D · 2669 Å² buried · 10 hydrogen bonds · protein-protein
A–D · 2665 Å² buried · 6 hydrogen bonds · protein-protein
A–B · 2659 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 2636 Å² buried · 6 hydrogen bonds · protein-protein
B–D · 31 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7XER · Structure of mTRPV2_Q525T · 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 0.96

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 7XER · PDBe 7XER · UniProt Q9WTR1

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