Target/Host (Institution) | Ligand | Target/Host Links | Ligand Links | Trg + Lig Links | Ki nM | ΔG° kJ/mole | IC50 nM | Kd nM | EC50/IC50 nM | koff s-1 | kon M-1s-1 | pH | Temp °C |
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Calmodulin-domain protein kinase 1 (481/484 > 99%)† (Toxoplasma gondii) | BDBM50345740 (3-(6-ethoxynaphthalen-2-yl)-1-isopropyl-1H-pyrazol...) | PDB UniProtKB/TrEMBL GoogleScholar AffyNet | Purchase CHEMBL MCE MMDB PC cid PC sid PDB UniChem Similars | PDB Article PubMed | n/a | n/a | 5 | n/a | n/a | n/a | n/a | n/a | n/a |
University of Washington. Curated by ChEMBL | Assay Description Inhibition of Toxoplasma gondii recombinant N-terminal hexahistidine tagged CDPK1 expressed in Escherichia coli using syntide-2 as substrate after 90... | ACS Med Chem Lett 1: 331-335 (2011) Article DOI: 10.1021/ml100096t BindingDB Entry DOI: 10.7270/Q2JW8FV5 | |||||||||||
More data for this Ligand-Target Pair | 3D Structure (crystal) | ||||||||||||
Calmodulin-domain protein kinase 1 (481/484 > 99%)† (Toxoplasma gondii) | BDBM50345740 (3-(6-ethoxynaphthalen-2-yl)-1-isopropyl-1H-pyrazol...) | PDB UniProtKB/TrEMBL GoogleScholar AffyNet | Purchase CHEMBL MCE MMDB PC cid PC sid PDB UniChem Similars | PDB US Patent | n/a | n/a | 5 | n/a | n/a | n/a | n/a | n/a | n/a |
UNIVERSITY OF WASHINGTON THROUGH ITS CENTER FOR CO US Patent | Assay Description Inhibition of TgCDPK1 and CpCDPK1 was determined using a luminescent kinase assay which measures ATP depletion in the presence of the Syntide 2 pepti... | US Patent US10544104 (2020) BindingDB Entry DOI: 10.7270/Q2D79DSF | |||||||||||
More data for this Ligand-Target Pair | 3D Structure (crystal) | ||||||||||||
Calmodulin-domain protein kinase 1 (481/484 > 99%)† (Toxoplasma gondii) | BDBM50345740 (3-(6-ethoxynaphthalen-2-yl)-1-isopropyl-1H-pyrazol...) | PDB UniProtKB/TrEMBL GoogleScholar AffyNet | Purchase CHEMBL MCE MMDB PC cid PC sid PDB UniChem Similars | PDB US Patent | n/a | n/a | 5 | n/a | n/a | n/a | n/a | n/a | n/a |
University of Washington Through its Center for Commercialization US Patent | Assay Description Most known kinase inhibitors bind in the ATP-binding pocket of the active site19,20. These inhibitors exploit many of the same hydrophobic contacts a... | US Patent US9765037 (2017) BindingDB Entry DOI: 10.7270/Q2B56MVC | |||||||||||
More data for this Ligand-Target Pair | 3D Structure (crystal) |