GL1X · GenesisL1 explorer

MolNFT v2 · #157152 · protein

cryo-EM structure of C-terminal truncated human Pannexin1

6LTN · Pannexin-1: “cryo-EM structure of C-terminal truncated human Pannexin1”. Electron microscopy at 3.1, 20 pockets (best druggability 0.77). MolNFT v2 #157152 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
6LTN
Type
protein
Length
1,708 residues
Chains
7
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.1
Source
Homo sapiens
Molecule
Pannexin-1
UniProt
Q96RD7
Pockets
20 · best druggability 0.77

Structure

electron microscopy · resolution 3.1 · 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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