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Cryo-EM structure of the ZAC zinc-activated channel in the Cys-loop receptor superfamily

Analyse Cryo-EM structure of the ZAC zinc-activated channel in the Cys-loop receptor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
8WGE
Type
protein
Length
1,740 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.4
Source
Oryzias latipes
Molecule
Zac
Ligands
NAG
Pockets
20 · best druggability 0.83

Structure

electron microscopy · resolution 3.4 · 1 distinct chain · 40% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, EZacprotein34840% helix, 27% strand—

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A, B, C, D, E

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

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111700.830.84125empty
24170.700.8038empty
35350.660.7777empty
43410.600.7846empty
53270.590.7853empty

Interfaces

5 interfaces between chains.

  • C–D · 2831 Ų buried · 24 hydrogen bonds · protein-protein
  • A–E · 2823 Ų buried · 23 hydrogen bonds · protein-protein
  • A–B · 2820 Ų buried · 25 hydrogen bonds · protein-protein
  • D–E · 2814 Ų buried · 24 hydrogen bonds · protein-protein
  • B–C · 2805 Ų buried · 24 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide, 5 glycan (disulfide, N-glycosylation).

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