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PORTAL

Analyse PORTAL in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7EY8
Type
protein
Length
6,300 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Portal protein
UniProt
P03728
Pockets
20 · best druggability 0.83

Structure

electron microscopy · 1 distinct chain · 48% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LPortal proteinprotein52548% helix, 11% strandP03728

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18730.830.8572empty
28280.820.8570empty
310310.820.8379empty
410280.820.8376empty
55940.820.8747empty

Interfaces

24 interfaces between chains.

  • K–L · 5973 Ų buried · 61 hydrogen bonds · protein-protein
  • E–F · 5970 Ų buried · 64 hydrogen bonds · protein-protein
  • J–K · 5964 Ų buried · 66 hydrogen bonds · protein-protein
  • A–L · 5964 Ų buried · 58 hydrogen bonds · protein-protein
  • A–B · 5963 Ų buried · 61 hydrogen bonds · protein-protein

Compared structures

  • 7EY8 · portal · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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