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GLUK3 receptor trapped in desensitized state

Analyse GLUK3 receptor trapped in desensitized state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6JFY
Type: protein
Length: 2,877 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamate receptor ionotropic, kainate 3
UniProt: P42264
Pockets: 20 · best druggability 0.86

Structure

electron microscopy · 3 distinct chains · 42% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D	Glutamate receptor ionotropic, kainate 3	protein	719	42% helix, 15% strand	P42264
A	Glutamate receptor ionotropic, kainate 3	protein	718	42% helix, 15% strand	P42264
C, B	Glutamate receptor ionotropic, kainate 3	protein	720	41% helix, 14% strand	P42264

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	618	0.86	0.91	90	empty
2	943	0.86	0.87	112	empty
3	933	0.85	0.85	103	empty
4	737	0.84	0.87	76	empty
5	398	0.83	0.91	64	empty

Interfaces

5 interfaces between chains.

D–C · 2757 Å² buried · 28 hydrogen bonds · protein-protein
A–B · 2606 Å² buried · 21 hydrogen bonds · protein-protein
D–A · 1185 Å² buried · 2 hydrogen bonds · protein-protein
C–B · 1021 Å² buried · 4 hydrogen bonds · protein-protein
D–B · 367 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

6JFY · GluK3 receptor trapped in Desensitized state · the same entry in another collection · chain A against A, TM-score 1.00
P42264 · AlphaFold monomer V2.0 prediction for glutamate receptor ionotropic, kainate 3 (P42264) · a predicted model of the same protein · chain A against A, TM-score 0.78

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 P42264
Elsewhere: RCSB PDB 6JFY · PDBe 6JFY · UniProt P42264

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