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Drug-Target Interaction

Drug

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PubChem ID:65056
Structure:
Synonyms:
863-03-6
Benzoic acid, 3,4,5-trihydroxy-,
Benzoic acid, 3,4,5-trihydroxy-, 2-(3,4-dihydroxyphenyl)-3,4-dihydro-5,7-dihydroxy-2H-1-benzopyran-3-yl ester, cis-
C15H14O6.C7H6O5
Epicatechin gallate
Epicatechin-3-gallate
Epicatechin-3-galloyl ester
LS-177919

Target

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Uniprot ID:Q7VFP2_HELHP
Synonyms:
DNA gyrase
EC-Numbers:5.99.1.3
Organism:Helicobacter hepaticus
PDB IDs:-

Binding Affinities:

Ki: Kd:Ic 50:Ec50/Ic50:
----

References:

17228868
Green tea catechins inhibit bacterial DNA gyrase by interaction with its ATP binding site.. Helena Gradisar; Primoz Pristovsek; Andreja Plaper; Roman Jerala (2007) Journal of medicinal chemistry display abstract
Catechins are the main ingredients of green tea extracts and have been shown to possess versatile biological activities, including antimicrobial. We determined that the catechins inhibit bacterial DNA gyrase by binding to the ATP binding site of the gyrase B subunit. In the group of four tested catechins, epigallocatechin gallate (EGCG) had the highest activity, followed by epicatechin gallate (ECG) and epigallocatechin (EGC). Specific binding to the N-terminal 24 kDa fragment of gyrase B was determined by fluorescence spectroscopy and confirmed using heteronuclear two-dimensional NMR spectroscopy of the EGCG-15N-labeled gyrase B fragment complex. Protein residues affected by binding to EGCG were identified through chemical shift perturbation. Molecular docking calculations suggest that the benzopyran ring of EGCG penetrates deeply into the active site while the galloyl moiety anchors it to the cleft through interactions with its hydroxyl groups, which explains the higher activity of EGCG and ECG.