MolNFT v1 · #168185 · protein

K2P2.1 (trek-1), 100 mm K+

6W83 · Potassium channel subfamily K member 2: “K2P2.1 (trek-1), 100 mm K+”. X-ray diffraction, 5 ligands (D12, R16, D10), 14 pockets (best druggability 0.77). MolNFT v1 #168185 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6W83
Type: protein
Length: 549 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Potassium channel subfamily K member 2
UniProt: P97438
Ligands: D12, R16, D10, K, CD
Pockets: 14 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Potassium channel subfamily K member 2	protein	268	75% helix, 0% strand	P97438
B	Potassium channel subfamily K member 2	protein	281	71% helix, 0% strand	P97438

Ligands and binding sites

D12 · Dodecane · ligand · 2 copies · chains A, B
R16 · Hexadecane · ligand · chains A, B
D10 · Decane · ligand · chains B
K · Potassium ion · metal · 6 copies · chains A, B
CD · Cadmium ion · metal · 3 copies · chains A, B
OCT · N-octane · additive · 3 copies · chains A

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

Pockets

14 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	1057	0.77	0.79	96	CD, K
2	76	0.67	0.92	19	empty
3	523	0.66	0.77	38	K
4	70	0.43	0.81	20	empty
5	54	0.36	0.78	12	empty

Interfaces

1 interface between chains.

A–B · 5148 Å² buried · 39 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6W83 · K2P2.1 (TREK-1), 100 mM K+ · the same entry in another collection · chain A against A, TM-score 1.00
P97438 · AlphaFold monomer V2.0 prediction for potassium channel subfamily K member 2 (P97438) · a predicted model of the same protein · chain B against A, TM-score 0.95

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 P97438
Elsewhere: RCSB PDB 6W83 · PDBe 6W83 · UniProt P97438

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