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Cryo-EM structure of C-terminal truncated human PANNEXIN1

Analyse Cryo-EM structure of C-terminal truncated human PANNEXIN1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LTN
Type
protein
Length
1,708 residues
Chains
7
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Pannexin-1
UniProt
Q96RD7
Pockets
20 · best druggability 0.77

Structure

electron microscopy · 1 distinct chain · 62% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
E, A, B, C, D, F, GPannexin-1protein24462% 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
110370.770.79126empty
2620.690.9621empty
3560.690.9627empty
4550.690.9622empty
54750.690.7956empty

Interfaces

7 interfaces between chains.

  • B–G · 1752 Ų buried · 8 hydrogen bonds · protein-protein
  • E–C · 1716 Ų buried · 8 hydrogen bonds · protein-protein
  • B–D · 1710 Ų buried · 8 hydrogen bonds · protein-protein
  • A–F · 1692 Ų buried · 9 hydrogen bonds · protein-protein
  • C–F · 1653 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

  • 6LTN · cryo-EM structure of C-terminal truncated human Pannexin1 · 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 E against A, TM-score 0.96

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