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BRENDA support

Literature summary for 3.4.21.5 extracted from

  • Engh, R.A.; Brandstetter, H.; Sucher, G.; Eichinger, A.; Baumann, U.; Bode, W.; Huber, R.; Poll, T.; Rudolph, R.; von der Saal, W.
    Enzyme flexibility, solvent and æweak' interactions characterize thrombin-ligand interactions: implications for drug design (1996), Structure, 4, 1353-1362.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information binding modes of a new class of orally available thrombin inhibitors based on 4-aminopyrimidine. Two inhibitors based on 4-aminopyridine bind in different ways. One forms a water-mediated hydrogen bond to the active site Ser195, the other induces a rotation of the Ser214-Trp215 peptide plane that is unprecedent in thrombin structures Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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