MolNFT v1 · #113700 · protein

Cryo-electron microscopy structure of rabbit TRPV2 ion channel

5AN8: “Cryo-electron microscopy structure of rabbit TRPV2 ion channel”. Electron microscopy, 20 pockets (best druggability 0.85). MolNFT v1 #113700 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5AN8
Type: protein
Length: 2,344 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TRPV2
UniProt: G1SNM3
Pockets: 20 · best druggability 0.85

Structure

electron microscopy · 1 distinct chain · 60% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	TRPV2	protein	586	60% helix, 2% strand	G1SNM3

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	955	0.85	0.86	109	empty
2	825	0.84	0.86	78	empty
3	978	0.84	0.85	93	empty
4	768	0.84	0.87	83	empty
5	1071	0.83	0.84	106	empty

Interfaces

6 interfaces between chains.

A–B · 1787 Å² buried · 2 hydrogen bonds · protein-protein
A–C · 1786 Å² buried · 2 hydrogen bonds · protein-protein
C–D · 1778 Å² buried · 2 hydrogen bonds · protein-protein
B–D · 1776 Å² buried · 2 hydrogen bonds · protein-protein
A–D · 30 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

5AN8 · Cryo-electron microscopy structure of rabbit TRPV2 ion channel · the same entry in another collection · chain A against A, TM-score 1.00

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 G1SNM3
Elsewhere: RCSB PDB 5AN8 · PDBe 5AN8 · UniProt G1SNM3

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