MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint barison-2009-1 Structural and mutational analysis of TenA protein (HP1287) from the Helicobacter pylori thiamin salvage pathway - evidence of a different substrate specificity. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Barison N., Cendron L., Trento A., Angelini A., Zanotti G. FEBS J. (1742-464X) 2009 Only protein-protein interactions imex curation o25874_helpy Aminopyrimidine aminohydrolase HP_1287 protein protein helpy Helicobacter pylori Campylobacter pylori MQVSQYLYQNVQSIWGDCISHPFVQGIGRGTLERDKFRFYIIQDYLFLLEYAKVFALGVVKACDEAVMREFSNAIQDILNNEMSIHNHYIRGLQITQKELQNARPTLANKSYTSYMLAEGFKGSIKEVAAAVLSCGWSYLVIAQNLSQIPNALEHAFYGHWIKGYSSKEFQACVNWNINLLDSLTLTSSKQEIEKLKDIFITTSEYEYLFWDMAYQS mint o25874 853700 o25874_helpy TenA 853701 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction false false false f2b mint