Found 14 Enz. Inhib. hit(s) with all data for entry = 2136 
Affinity DataKi: 0.110nM ΔG°: -56.3kJ/molepH: 7.5 T: 2°CAssay 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...More data for this Ligand-Target Pair
Affinity DataKi: 0.270nM ΔG°: -54.1kJ/molepH: 7.5 T: 2°CAssay 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...More data for this Ligand-Target Pair
Affinity DataKi: 0.660nM ΔG°: -51.9kJ/molepH: 7.5 T: 2°CAssay 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...More data for this Ligand-Target Pair
Affinity DataKi: 1.60nM ΔG°: -49.7kJ/molepH: 7.5 T: 2°CAssay 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...More data for this Ligand-Target Pair
Affinity DataKi: 14nM ΔG°: -44.4kJ/molepH: 7.5 T: 2°CAssay 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...More data for this Ligand-Target Pair
Affinity DataKi: 18nM ΔG°: -43.8kJ/molepH: 7.5 T: 2°CAssay 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...More data for this Ligand-Target Pair
3D Structure (crystal)
Affinity DataKi: 20nM ΔG°: -43.5kJ/molepH: 7.5 T: 2°CAssay 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...More data for this Ligand-Target Pair
Affinity DataKi: 33nM ΔG°: -42.3kJ/molepH: 7.5 T: 2°CAssay 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...More data for this Ligand-Target Pair
Affinity DataKi: 36nM ΔG°: -42.1kJ/molepH: 7.5 T: 2°CAssay 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...More data for this Ligand-Target Pair
Affinity DataKi: 85nM ΔG°: -40.0kJ/molepH: 7.5 T: 2°CAssay 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...More data for this Ligand-Target Pair
Affinity DataKi: 170nM ΔG°: -38.2kJ/molepH: 7.5 T: 2°CAssay 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...More data for this Ligand-Target Pair
Affinity DataKi: 200nM ΔG°: -37.9kJ/molepH: 7.5 T: 2°CAssay 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...More data for this Ligand-Target Pair
Affinity DataKi: 870nM ΔG°: -34.2kJ/molepH: 7.5 T: 2°CAssay 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...More data for this Ligand-Target Pair
Affinity DataKi: 1.40E+3nM ΔG°: -33.1kJ/molepH: 7.5 T: 2°CAssay 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...More data for this Ligand-Target Pair
