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cryo-EM structure of human Pannexin 1 channel

Analyse cryo-EM structure of human Pannexin 1 channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6M02
Type
protein
Length
2,345 residues
Chains
7
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.2
Source
Homo sapiens
Molecule
Pannexin-1
UniProt
Q96RD7
Pockets
20 · best druggability 0.77

Structure

electron microscopy · resolution 3.2 · 1 distinct chain · 51% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, GPannexin-1protein33551% helix, 4% strandQ96RD7

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1850.770.9819empty
27620.770.8182empty
3890.770.9819empty
41750.770.9325empty
57560.770.8176empty

Interfaces

7 interfaces between chains.

  • A–G · 2880 Ų buried · 13 hydrogen bonds · protein-protein
  • A–B · 2878 Ų buried · 13 hydrogen bonds · protein-protein
  • B–C · 2876 Ų buried · 14 hydrogen bonds · protein-protein
  • D–E · 2874 Ų buried · 13 hydrogen bonds · protein-protein
  • E–F · 2872 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 disulfide (disulfide).

Compared structures

  • 6M02 · Cryo-EM structure of human pannexin 1 channel · the same entry in another collection · chain G against G, TM-score 1.00
  • Q96RD7 · AlphaFold monomer V2.0 prediction for pannexin-1 (Q96RD7) · a predicted model of the same protein · chain A against A, TM-score 0.86

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