Crystallization (Comment) | Organism |
---|---|
modeling of complex with inhibitor epigallocatechin-3-gallate. The presence of epigallocatechin-3-gallate contiguous to the active site entrance leads to the movement of several residues in the active site. Epigallocatechin-3-gallate occludes the entrance channel to the enzyme active site and establishes new interactions with residues in the active site. These residues turn outward when the active site collapses | Rattus norvegicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
epigallocatechin-3-gallate | direct inhibitory effect on both histidine decarboxylase and DOPA decarboxylase. Modeling of binding to the enzymes. The presence of epigallocatechin-3-gallate contiguous to the active site entrance leads to the movement of several residues in the active site. Epigallocatechin-3-gallate occludes the entrance channel to the enzyme active site and establishes new interactions with residues in the active site. These residues turn outward when the active site collapses. After docking of epigallocatechin-3-gallate, neither histidine nor the inhibitors histidine methyl ester and alpha-fluoromethyl histidine are able to bind to the enzyme | Rattus norvegicus |
Organism | UniProt | Comment | Textmining |
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Rattus norvegicus | - |
- |
- |