Research workbench
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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pleckstrin homology domain-containing family a member 8 | protein | 211 | 68% helix, 3% strand | Q96JA3 |
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 711 | 0.88 | 0.91 | 71 | 6S8 |
| 2 | 367 | 0.84 | 0.92 | 45 | 6S8 |
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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q96JA3
- Elsewhere: RCSB PDB 5KDI · PDBe 5KDI · UniProt Q96JA3
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