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How FAPP2 selects simple glycosphingolipids using the gltp-fold

Analyse How FAPP2 selects simple glycosphingolipids using the gltp-fold in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5KDI
Type
protein
Length
422 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Pleckstrin homology domain-containing family a member 8
UniProt
Q96JA3
Ligands
6S8
Pockets
2 · best druggability 0.88

Structure

x-ray diffraction · 1 distinct chain · 68% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPleckstrin homology domain-containing family a member 8protein21168% helix, 3% strandQ96JA3

Ligands and binding sites

  • 6S8 · (~{Z})-~{N}-[(~{E},2~{S},3~{R})-1-[(2~{R},3~{R},4~{S}, 5~{R},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl) oxan-2-yl]oxy-3-oxidanyl-octadec-4-en-2-yl]octadec-9-enamide · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17110.880.91716S8
23670.840.92456S8

Interfaces

1 interface between chains.

  • A–B · 1096 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 5KDI · How FAPP2 Selects Simple Glycosphingolipids Using the GLTP-fold · the same entry in another collection · chain A against A, TM-score 1.00
  • Q96JA3 · AlphaFold monomer V2.0 prediction for pleckstrin homology domain- containing family a… · a predicted model of the same protein · chain A against A, TM-score 0.98

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