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 Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi. Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi. J. Mol. Biol. (0022-2836) 1995 Baumann U., Bauer M., Létoffé S., Delepelaire P., Wandersman C. no in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Baumann U., Bauer M., Létoffé S., Delepelaire P., Wandersman C. no J. Mol. Biol. (0022-2836) 1995 przn_serma Serralysin Extracellular metalloproteinase Zinc proteinase protein protein serma Serratia marcescens MQSTKKAIEITESSLAAATTGYDAVDDLLHYHERGNGIQINGKDSFSNEQAGLFITRENQTWNGYKVFGQPVKLTFSFPDYKFSSTNVAGDTGLSKFSAEQQQQAKLSLQSWADVANITFTEVAAGQKANITFGNYSQDRPGHYDYGTQAYAFLPNTIWQGQDLGGQTWYNVNQSNVKHPATEDYGRQTFTHEIGHALGLSHPGDYNAGEGNPTYNDVTYAEDTRQFSLMSYWSETNTGGDNGGHYAAAPLLDDIAAIQHLYGANPSTRTGDTVYGFNSNTGRDFLSTTSNSQKVIFAAWDAGGNDTFDFSGYTANQRINLNEKSFSDVGGLKGNVSIAAGVTIENAIGGSGNDVIVGNAANNVLKGGAGNDVLFGGGGADELWGGAGKDIFVFSAASDSAPGASDWIRDFQKGIDKIDLSFFNKEANSSDFIHFVDHFSGTAGEALLSYNASSNVTDLSVNIGGHQAPDFLVKIVGQVDVATDFIV mint Has insecticidal activity against the locust M.palpalis. When administered orally to locusts at a low dose it causes them to lie on their sides exhibiting sporadic limb movements and muscular twitching, followed by full recovery. When administered at higher doses the same symptoms are observed, followed by death 8689FC84D83CAA2C inh_dicch Proteinase inhibitor inh protein protein erwch Erwinia chrysanthemi Pectobacterium chrysanthemi Erwinia chrysanthemi MKQLIIATLLSALSGGCMASSLRLPSAAELSGQWVLSGAEQHCDIRLNTDVLDGTTWKLAGDTACLQKLLPEAPVGWRPTPDGLTLTQADGSAVAFFSRNRDRYEHKLVDGSVRTLKKKA mint Inhibitor of the extracellular proteases A, B, and C of E.chrysanthemi and the S.marcescens 50 kDa extracellular protease. It forms a non-covalent bond with the proteases and may prevent autocatalytic cleavage of the proteases zymogen in the periplasm F73BB59026E069D1 inh-przn 1 2 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 direct interaction direct interaction In the xray complex 1smp, P23694 is chain A and P18958 is chain I Resolution 2.300 mint