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Phosphorylated trif in complex with irf-3

Analyse Phosphorylated trif in complex with irf-3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5JEL
Type
protein
Length
248 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Interferon regulatory factor 3; Phosphorylated trif peptide
UniProt
Q14653
Pockets
1 · best druggability 0.31

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInterferon regulatory factor 3protein23426% helix, 32% strandQ14653
BPhosphorylated trif peptideprotein1450% helix, 14% strand—

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1790.310.7314empty

Interfaces

1 interface between chains.

  • A–B · 658 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (phosphorylation).

Compared structures

  • 5JEL · Phosphorylated TRIF in complex with IRF-3 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q14653 · AlphaFold monomer V2.0 prediction for interferon regulatory factor 3 (Q14653) · a predicted model of the same protein · chain A against A, TM-score 0.99

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