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The flattened structure of MPIEZO1 in lipid bilayer

Analyse The flattened structure of MPIEZO1 in lipid bilayer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7WLU
Type
protein
Length
4,494 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Piezo-type mechanosensitive ion channel component 1
UniProt
E2JF22
Ligands
PLX
Pockets
20 · best druggability 0.88

Structure

electron microscopy · 1 distinct chain · 66% helix, 6% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, EPiezo-type mechanosensitive ion channel component 1protein149866% helix, 6% strandE2JF22

Ligands and binding sites

  • PLX · (9R,11S)-9-({[(1S)-1-hydroxyhexadecyl]oxy}methyl)-2,2-dimethyl-5,7,10-trioxa-2lambda~5~-aza-6lambda~5~-phosphaoctacosane-6,6,11-triol · ligand · 3 copies · chains A, C, 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, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111580.880.88127empty
210350.870.88118empty
311880.860.86110empty
412000.860.86117empty
56030.850.9052empty

Interfaces

3 interfaces between chains.

  • A–C · 2410 Ų buried · 18 hydrogen bonds · protein-protein
  • A–E · 2409 Ų buried · 18 hydrogen bonds · protein-protein
  • C–E · 2404 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 7WLU · The Flattened Structure of mPIEZO1 in Lipid Bilayer · the same entry in another collection · chain A against A, TM-score 1.00
  • E2JF22 · AlphaFold monomer V2.0 prediction for piezo-type mechanosensitive ion channel component 1… · a predicted model of the same protein · chain A against A, TM-score 0.70

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