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Structure of the FAS/FADD death domain assembly

Analyse Structure of the FAS/FADD death domain assembly in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OQ9
Type
protein
Length
890 residues
Chains
10
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tumor necrosis factor receptor superfamily member 6; Protein fadd
UniProt
P25446, Q13158
Pockets
12 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, ETumor necrosis factor receptor superfamily member 6protein8669% helix, 0% strandP25446
H, I, J, K, LProtein faddprotein9273% helix, 0% strandQ13158

Pockets

12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14880.830.9070empty
23730.830.9159empty
34840.820.8958empty
43610.780.8858empty
53940.780.8760empty

Interfaces

28 interfaces between chains.

  • B–C · 480 Ų buried · 6 hydrogen bonds · protein-protein
  • E–L · 464 Ų buried · 5 hydrogen bonds · protein-protein
  • C–D · 446 Ų buried · 11 hydrogen bonds · protein-protein
  • D–K · 423 Ų buried · 2 hydrogen bonds · protein-protein
  • A–B · 414 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 3OQ9 · Structure of the FAS/FADD death domain assembly · the same entry in another collection · chain L against L, TM-score 1.00
  • Q13158 · AlphaFold monomer V2.0 prediction for fas-associated death domain protein (Q13158) · a predicted model of the same protein · chain I against A, TM-score 0.95

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