Structure of the regulatory fragment of saccharomyces cerevisiae ampk in complex with ADP

Structure

x-ray diffraction · 3 distinct chains · 43% helix, 25% strand (DSSP).

Ligands and binding sites

• ADP · Adenosine-5'-diphosphate · ligand · chains C

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

3 interfaces between chains.

• A–B · 2576 Ų buried · 34 hydrogen bonds · protein-protein
• A–C · 1941 Ų buried · 28 hydrogen bonds · protein-protein
• B–C · 1016 Ų buried · 20 hydrogen bonds · protein-protein

Compared structures

• 3T4N · Structure of the regulatory fragment of Saccharomyces cerevisiae AMPK in complex with ADP · the same entry in another collection · chain A against A, TM-score 1.00
• P12904 · AlphaFold monomer V2.0 prediction for 5'-AMP-activated protein kinase subunit gamma… · a predicted model of the same protein · chain C against A, TM-score 0.94
• P34164 · AlphaFold monomer V2.0 prediction for SNF1 protein kinase subunit beta-2 (P34164) · a predicted model of the same protein · chain B against A, TM-score 0.79
• P06782 · AlphaFold monomer V2.0 prediction for carbon catabolite-derepressing protein kinase… · a predicted model of the same protein · chain A against A, TM-score 0.73

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 P06782
• Every structure of UniProt P34164
• Every structure of UniProt P12904
• Elsewhere: RCSB PDB 3T4N · PDBe 3T4N · UniProt P06782 · UniProt P34164 · UniProt P12904