GL1X · GenesisL1 explorer

Research workbench

Complex ggnn of AMPA-subtype iglur GLUA2 in complex with auxiliary subunit GAMMA2 (stargazin) at low glutamate concentration (20 um) in the presence of cyclothiazide (100 um)

Analyse Complex ggnn of AMPA-subtype iglur GLUA2 in complex with auxiliary subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7TNN
Type
protein
Length
2,484 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Isoform flip of glutamate receptor 2,VOLTAGE-dependent calcium channel gamma-3 subunit…
UniProt
P19491
Ligands
CYZ, GLU
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 4 distinct chains · 50% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AIsoform flip of glutamate receptor 2,VOLTAGE-dependent calcium channel gamma-3 subunit chimeraprotein61950% helix, 12% strandP19491
BIsoform flip of glutamate receptor 2,VOLTAGE-dependent calcium channel gamma-3 subunit chimeraprotein62149% helix, 12% strandP19491
CIsoform flip of glutamate receptor 2,VOLTAGE-dependent calcium channel gamma-3 subunit chimeraprotein62451% helix, 12% strandP19491
DIsoform flip of glutamate receptor 2,VOLTAGE-dependent calcium channel gamma-3 subunit chimeraprotein62049% helix, 12% strandP19491

Ligands and binding sites

  • CYZ · Cyclothiazide · ligand · 4 copies · chains A, D, B, C
  • GLU · Glutamic acid · ligand · 2 copies · chains A, B

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

Pockets

20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111950.840.85132empty
28440.810.8488empty
37330.800.8488CYZ
411840.800.81125CYZ
59850.770.7996empty

Interfaces

4 interfaces between chains.

  • A–D · 4009 Ų buried · 27 hydrogen bonds · protein-protein
  • B–C · 3878 Ų buried · 16 hydrogen bonds · protein-protein
  • A–B · 3030 Ų buried · 12 hydrogen bonds · protein-protein
  • C–D · 2977 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

  • 7TNN · Complex GGNN of AMPA-subtype iGluR GluA2 in complex with auxiliary subunit gamma2… · the same entry in another collection · chain D against D, TM-score 1.00
  • P19491 · AlphaFold monomer V2.0 prediction for glutamate receptor 2 (P19491) · a predicted model of the same protein · chain B against A, TM-score 0.62

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.