Structural basis for differential recognition of tyrosine phosphorylated sites in the linker for activation of T cells (lat) by the adaptor protein gads

Structure

x-ray diffraction · 3 distinct chains · 18% helix, 23% strand (DSSP).

Ligands and binding sites

• ACE · Acetyl group · ligand · 2 copies · chains A, B, C, D
• SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D

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

Pockets

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

Interfaces

4 interfaces between chains.

• A–C · 494 Ų buried · 18 hydrogen bonds · protein-protein
• B–D · 461 Ų buried · 12 hydrogen bonds · protein-protein
• A–B · 193 Ų buried · 1 hydrogen bond · protein-protein
• B–C · 115 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent, 2 modified (covalent ligand, phosphorylation).

Compared structures

• 1R1Q · Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the… · the same entry in another collection · chain A against A, TM-score 1.00
• O89100 · AlphaFold monomer V2.0 prediction for GRB2-related adaptor protein 2 (O89100) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 O89100
• Elsewhere: RCSB PDB 1R1Q · PDBe 1R1Q · UniProt O89100