Compile Data Set for Download or QSAR
Report error Found 26 Enz. Inhib. hit(s) with all data for entry = 50018789
TargetAmine oxidase [flavin-containing] A(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 100152BDBM100152(cid_5359389 | SMR001233259 | HARMINE | 7-methoxy-1...)
Affinity DataIC50: 4.10nMAssay Description:Inhibition of human recombinant MAO-A assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] A(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612564BDBM50612564(CHEMBL5286089)
Affinity DataIC50: 724nMAssay Description:Inhibition of human recombinant MAO-A assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] A(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612569BDBM50612569(CHEMBL5286143)
Affinity DataIC50: 1.21E+3nMAssay Description:Inhibition of human recombinant MAO-A assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] A(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612568BDBM50612568(CHEMBL5281498)
Affinity DataIC50: 1.68E+3nMAssay Description:Inhibition of human recombinant MAO-A assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] A(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50609172BDBM50609172(CHEMBL5278584)
Affinity DataIC50: 2.03E+3nMAssay Description:Inhibition of human recombinant MAO-A assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] B(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612568BDBM50612568(CHEMBL5281498)
Affinity DataIC50: 2.79E+3nMAssay Description:Inhibition of human recombinant MAO-B assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] A(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612563BDBM50612563(CHEMBL5279074)
Affinity DataIC50: 3.89E+3nMAssay Description:Inhibition of human recombinant MAO-A assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] B(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 11022BDBM11022(2,3-dihydro-1H-indole-2,3-dione | CHEMBL326294 | I...)
Affinity DataIC50: 3.90E+3nMAssay Description:Inhibition of human recombinant MAO-B assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMedPDB3D3D Structure (crystal)
TargetAmine oxidase [flavin-containing] A(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612562BDBM50612562(CHEMBL1159896)
Affinity DataIC50: 4.72E+3nMAssay Description:Inhibition of human recombinant MAO-A assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] A(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612567BDBM50612567(CHEMBL5285077)
Affinity DataIC50: 5.17E+3nMAssay Description:Inhibition of human recombinant MAO-A assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] A(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612573BDBM50612573(CHEMBL5286181)
Affinity DataIC50: 6.66E+3nMAssay Description:Inhibition of human recombinant MAO-A assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] A(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612571BDBM50612571(CHEMBL5280535)
Affinity DataIC50: 7.15E+3nMAssay Description:Inhibition of human recombinant MAO-A assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] A(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612565BDBM50612565(CHEMBL5287493)
Affinity DataIC50: 7.82E+3nMAssay Description:Inhibition of human recombinant MAO-A assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] A(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 11022BDBM11022(2,3-dihydro-1H-indole-2,3-dione | CHEMBL326294 | I...)
Affinity DataIC50: 8.43E+3nMAssay Description:Inhibition of human recombinant MAO-A assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] A(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612566BDBM50612566(CHEMBL5279171)
Affinity DataIC50: 9.79E+3nMAssay Description:Inhibition of human recombinant MAO-A assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] A(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612570BDBM50612570(CHEMBL5270139)
Affinity DataIC50: 1.05E+4nMAssay Description:Inhibition of human recombinant MAO-A assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] B(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612570BDBM50612570(CHEMBL5270139)
Affinity DataIC50: 1.34E+4nMAssay Description:Inhibition of human recombinant MAO-B assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] A(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612574BDBM50612574(CHEMBL5270106)
Affinity DataIC50: 1.40E+4nMAssay Description:Inhibition of human recombinant MAO-A assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] B(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612567BDBM50612567(CHEMBL5285077)
Affinity DataIC50: 1.67E+4nMAssay Description:Inhibition of human recombinant MAO-B assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] B(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612571BDBM50612571(CHEMBL5280535)
Affinity DataIC50: 2.13E+4nMAssay Description:Inhibition of human recombinant MAO-B assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] A(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612572BDBM50612572(CHEMBL5270587)
Affinity DataIC50: 2.54E+4nMAssay Description:Inhibition of human recombinant MAO-A assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] B(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50609172BDBM50609172(CHEMBL5278584)
Affinity DataIC50: 3.65E+4nMAssay Description:Inhibition of human recombinant MAO-B assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] B(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612569BDBM50612569(CHEMBL5286143)
Affinity DataIC50: 3.68E+4nMAssay Description:Inhibition of human recombinant MAO-B assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] B(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612562BDBM50612562(CHEMBL1159896)
Affinity DataIC50: 5.73E+4nMAssay Description:Inhibition of human recombinant MAO-B assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] B(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612564BDBM50612564(CHEMBL5286089)
Affinity DataIC50: 6.48E+4nMAssay Description:Inhibition of human recombinant MAO-B assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed
TargetAmine oxidase [flavin-containing] B(Human)
University of Florence

Curated by ChEMBL
LigandChemical structure of BindingDB Monomer ID 50612574BDBM50612574(CHEMBL5270106)
Affinity DataIC50: 8.42E+4nMAssay Description:Inhibition of human recombinant MAO-B assessed as inhibition of 4-hydroxyquinoline formation using kynuramine as substrate by fluorescence spectropho...More data for this Ligand-Target Pair
In Depth
Date in BDB:
4/21/2024
Entry Details
PubMed