Crystal structures of the kinase domain of AKT2 in complex with ATP- competitive inhibitors

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 18% strand (DSSP).

Ligands and binding sites

• G96 · 4-[2-(4-amino-1,2,5-oxadiazol-3-yl)-6-{[(2R)-2-amino-3-phenylpropyl]oxy}-1-ethyl-1H-imidazo[4,5-c]pyridin-4-yl]-2-methylbut-3-yn-2-ol · ligand · 2 copies · chains A, C, B, D

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

Pockets

10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Interfaces

4 interfaces between chains.

• B–D · 738 Ų buried · 16 hydrogen bonds · protein-protein
• A–C · 736 Ų buried · 18 hydrogen bonds · protein-protein
• A–B · 543 Ų buried · 1 hydrogen bond · protein-protein
• B–C · 142 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (phosphorylation).

Compared structures

• 3E88 · Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors · the same entry in another collection · chain A against A, TM-score 1.00
• P31751 · AlphaFold monomer V2.0 prediction for rac-beta SERINE/THREONINE- protein kinase (P31751) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 P31751
• Every structure of UniProt P49841
• Elsewhere: RCSB PDB 3E88 · PDBe 3E88 · UniProt P31751 · UniProt P49841