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TASK2 in MSP1D1 lipid nanodisc at pH 8.5

Analyse TASK2 in MSP1D1 lipid nanodisc at pH 8.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WM0
Type: protein
Length: 510 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Potassium channel TASK2
UniProt: Q9JK62
Ligands: K
Pockets: 10 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Potassium channel TASK2	protein	255	73% helix, 0% strand	Q9JK62

Ligands and binding sites

K · Potassium ion · metal · 5 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1110	0.78	0.80	79	K
2	1049	0.77	0.79	64	empty
3	82	0.74	0.96	23	empty
4	197	0.48	0.75	31	empty
5	166	0.45	0.75	21	empty

Interfaces

1 interface between chains.

A–B · 4856 Å² buried · 24 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6WM0 · TASK2 in MSP1D1 lipid nanodisc at pH 8.5 · 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 Q9JK62
Elsewhere: RCSB PDB 6WM0 · PDBe 6WM0 · UniProt Q9JK62

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