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Cryo-EM structure of human pannexin 1 channel with deletion of N- terminal helix and C-terminal tail

Analyse Cryo-EM structure of human pannexin 1 channel with deletion of N- terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6WBK
Type
protein
Length
2,181 residues
Chains
7
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Pannexin-1
UniProt
Q96RD7
Pockets
20 · best druggability 0.81

Structure

electron microscopy · 5 distinct chains · 66% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPannexin-1protein31565% helix, 4% strandQ96RD7
C, FPannexin-1protein30968% helix, 3% strandQ96RD7
DPannexin-1protein31267% helix, 4% strandQ96RD7
EPannexin-1protein30866% helix, 4% strandQ96RD7
GPannexin-1protein31366% helix, 3% strandQ96RD7

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15840.810.87127empty
24540.800.8896empty
34270.780.8793empty
44120.780.8781empty
53360.770.8865empty

Interfaces

7 interfaces between chains.

  • C–D · 844 Ų buried · 0 hydrogen bonds · protein-protein
  • F–G · 824 Ų buried · 2 hydrogen bonds · protein-protein
  • B–C · 799 Ų buried · 0 hydrogen bonds · protein-protein
  • A–G · 779 Ų buried · 0 hydrogen bonds · protein-protein
  • E–F · 678 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6WBK · Cryo-EM structure of human Pannexin 1 channel with deletion of N-terminal helix and… · 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 C against A, TM-score 0.98

Analyse

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