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 |
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Coagulation factor X (52/52 = 100%)† (Homo sapiens (Human)) | BDBM17135 (3-chloro-N-{4-chloro-2-[(5-chloropyridin-2-yl)carb...) | PDB MMDB Reactome pathway KEGG UniProtKB/SwissProt B.MOAD DrugBank antibodypedia GoogleScholar AffyNet | MMDB PC cid PC sid PDB UniChem Patents Similars | MMDB PDB Article PubMed | 0.00500 | n/a | n/a | n/a | n/a | n/a | n/a | n/a | n/a |
Berlex Biosciences | Assay Description The enzyme activities were determined kinetically as the initial rate of cleavage of a peptide p-nitroanilide. Km for enzyme and substrate was determ... | J Med Chem 50: 2967-80 (2007) Article DOI: 10.1021/jm070125f BindingDB Entry DOI: 10.7270/Q2J101F5 | |||||||||||
More data for this Ligand-Target Pair | 3D Structure (crystal) | ||||||||||||
Coagulation factor X (52/52 = 100%)† (Homo sapiens (Human)) | BDBM17135 (3-chloro-N-{4-chloro-2-[(5-chloropyridin-2-yl)carb...) | PDB MMDB Reactome pathway KEGG UniProtKB/SwissProt B.MOAD DrugBank antibodypedia GoogleScholar AffyNet | MMDB PC cid PC sid PDB UniChem Patents Similars | MMDB PDB Article PubMed | 0.00500 | n/a | n/a | n/a | n/a | n/a | n/a | n/a | n/a |
Bristol-Myers Squibb Company Curated by ChEMBL | Assay Description Inhibition of factor 10a | J Med Chem 53: 6243-74 (2010) Article DOI: 10.1021/jm100146h BindingDB Entry DOI: 10.7270/Q2CR5VBB | |||||||||||
More data for this Ligand-Target Pair | 3D Structure (crystal) | ||||||||||||
Coagulation factor X (203/234 = 87%)† (Rattus norvegicus (rat)) | BDBM17135 (3-chloro-N-{4-chloro-2-[(5-chloropyridin-2-yl)carb...) | PDB MMDB Reactome pathway KEGG UniProtKB/SwissProt B.MOAD GoogleScholar AffyNet | MMDB PC cid PC sid PDB UniChem Patents Similars | MMDB PDB Article PubMed | 0.0600 | n/a | n/a | n/a | n/a | n/a | n/a | n/a | n/a |
Berlex Biosciences | Assay Description The enzyme activities were determined kinetically as the initial rate of cleavage of a peptide p-nitroanilide. Km for enzyme and substrate was determ... | J Med Chem 50: 2967-80 (2007) Article DOI: 10.1021/jm070125f BindingDB Entry DOI: 10.7270/Q2J101F5 | |||||||||||
More data for this Ligand-Target Pair | 3D Structure (crystal) |