MolNFT v2 · #211144 · protein

GluK1-1a receptor captured in the desensitized state

8GPR · Glutamate receptor: “GluK1-1a receptor captured in the desensitized state”. Electron microscopy at 8.2, 20 pockets (best druggability 0.85). MolNFT v2 #211144 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 8GPR
Type: protein
Length: 2,948 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 8.2
Source: Rattus norvegicus
Molecule: Glutamate receptor
UniProt: A0A0G2K830
Pockets: 20 · best druggability 0.85

Structure

electron microscopy · resolution 8.2 · 1 distinct chain · 41% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Glutamate receptor	protein	737	41% helix, 18% strand	A0A0G2K830

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	888	0.85	0.87	134	empty
2	801	0.84	0.86	75	empty
3	731	0.83	0.86	111	empty
4	227	0.83	0.95	48	empty
5	878	0.82	0.85	99	empty

Interfaces

5 interfaces between chains.

C–D · 3531 Å² buried · 34 hydrogen bonds · protein-protein
A–B · 2835 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 1467 Å² buried · 6 hydrogen bonds · protein-protein
A–D · 1247 Å² buried · 15 hydrogen bonds · protein-protein
B–D · 560 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

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 A0A0G2K830
Elsewhere: RCSB PDB 8GPR · PDBe 8GPR · UniProt A0A0G2K830

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