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 sheffield-2001-1 Preparation and crystal structure of the recombinant alpha(1)/alpha(2) catalytic heterodimer of bovine brain platelet-activating factor acetylhydrolase Ib. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Sheffield PJ., McMullen TW., Li J., Ho YS., Garrard SM., Derewenda U., Derewenda ZS. PDBe - Data obtained from the Protein Data Bank Europe Protein Eng. (0269-2139) 2001 pa1b2_bovin Platelet-activating factor acetylhydrolase IB subunit alpha2 PAFAH1B2P68402 PAF acetylhydrolase 30 kDa subunit PAF-AH subunit beta PAFAHB protein protein bovin Bos taurus (Bovine) Bovine MSQGDSNPAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQYEIWRELFSPLHALNFGIGGDTTRHVLWRLKNGELENIKPKVIVVWVGTNNHENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDTDGGFVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEETPEEKQTTIA pa1b3_bovin Platelet-activating factor acetylhydrolase IB subunit alpha1 PAFAH1B3 PAFAHG PAF acetylhydrolase 29 kDa subunit PAF-AH subunit gamma protein protein bovin Bos taurus (Bovine) Bovine MSGDENPASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQCEIWRELFSPLHALNFGIGGDSTQHVLWRLENGELEHIRPKIVVVWVGTNNHGHTAEQVTGGIKAIVQLVNERQPQARVVVLGLLPRGQHPNPLREKNRRVNELVRAALAGHPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVCRALHSLLLRLLTQDQGQGGAPLPEPSP pafah1b2-pafah1b3-1 Crystal structure of the recombinant alpha1/alpha2 catalytic heterodimer of bovine brain platelet-activating factor acetylhydrolase ib. 99739 N/A 99740 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 1.0 N/A 99741 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 1.0 direct interaction direct interaction false false false dimeric, multimeric working 78.200%, free 72.500% 2.1A