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Cryo-EM structure of a de novo designed 16-helix transmembrane nanopore, TMHC8_R.

Analyse Cryo-EM structure of a de novo designed 16-helix transmembrane nanopore… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6U1S
Type
protein
Length
2,480 residues
Chains
8
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
De novo designed 16-helix transmembrane nanopore, TMHC8_R
Pockets
20 · best druggability 0.76

Structure

electron microscopy · 1 distinct chain · 89% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, D, F, H, J, L, NDe novo designed 16-helix transmembrane nanopore, TMHC8_Rprotein31089% helix, 0% strand—

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18480.760.8095empty
27780.760.8188empty
38430.750.7992empty
48240.750.7988empty
58270.750.7982empty

Interfaces

8 interfaces between chains.

  • A–N · 2863 Ų buried · 30 hydrogen bonds · protein-protein
  • J–L · 2862 Ų buried · 30 hydrogen bonds · protein-protein
  • F–H · 2858 Ų buried · 30 hydrogen bonds · protein-protein
  • D–F · 2858 Ų buried · 30 hydrogen bonds · protein-protein
  • H–J · 2856 Ų buried · 30 hydrogen bonds · protein-protein

Compared structures

  • 6U1S · Cryo-EM structure of a de novo designed 16-helix transmembrane nanopore, TMHC8_R. · the same entry in another collection · chain A against A, TM-score 1.00

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