5A6O

Crystal structure of the apo form of the unphosphorylated human death associated protein kinase 3 (DAPK3)

Summary for 5A6O

• Entry DOI: 10.2210/pdb5a6o/pdb
• Related: 5A6N
• Descriptor: DEATH-ASSOCIATED PROTEIN KINASE 3, GLYCEROL, S-1,2-PROPANEDIOL, ... (4 entities in total)
• Functional Keywords: transferase, dapk3, apo, death-associated protein kinase 3, zipper-interacting protein kinase
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Nucleus . Isoform 1: Nucleus . Isoform 2: Nucleus : O43293
• Total number of polymer chains: 2
• Total formula weight: 65518.72

Authors

Rodrigues, T.,Reker, D.,Welin, M.,Caldera, M.,Brunner, C.,Gabernet, G.,Schneider, P.,Walse, B.,Schneider, G. (deposition date: 2015-06-30, release date: 2015-10-21, Last modification date: 2024-01-10)

Primary citation

Rodrigues, T.,Reker, D.,Welin, M.,Caldera, M.,Brunner, C.,Gabernet, G.,Schneider, P.,Walse, B.,Schneider, G.
De Novo Fragment Design for Drug Discovery and Chemical Biology.
Angew.Chem.Int.Ed.Engl., 54:15079-, 2015

PubMed Abstract: Automated molecular de novo design led to the discovery of an innovative inhibitor of death-associated protein kinase 3 (DAPK3). An unprecedented crystal structure of the inactive DAPK3 homodimer shows the fragment-like hit bound to the ATP pocket. Target prediction software based on machine learning models correctly identified additional macromolecular targets of the computationally designed compound and the structurally related marketed drug azosemide. The study validates computational de novo design as a prime method for generating chemical probes and starting points for drug discovery.

PubMed: 26486226
DOI: 10.1002/ANIE.201508055

Experimental method

X-RAY DIFFRACTION (1.6 Å)