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 bell-2002-1 3-Aminopyrrolidinone farnesyltransferase inhibitors: design of macrocyclic compounds with improved pharmacokinetics and excellent cell potency. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Bell IM., Gallicchio SN., Abrams M., Beese LS., Beshore DC., Bhimnathwala H., Bogusky MJ., Buser CA., Culberson JC., Davide J., Ellis-Hutchings M., Fernandes C., Gibbs JB., Graham SL., Hamilton KA., Hartman GD., Heimbrook DC., Homnick CF., Huber HE., Huff JR., Kassahun K., Koblan KS., Kohl NE., Lobell RB., Lynch JJ., Robinson R., Rodrigues AD., Taylor JS., Walsh ES., Williams TM., Zartman CB. PDBe - Data obtained from the Protein Data Bank Europe ian_bell@merck.com J. Med. Chem. (0022-2623) 2002 fntb_human Protein farnesyltransferase subunit beta CAAX farnesyltransferase subunit beta Ras proteins prenyltransferase subunit beta FNTB protein protein human Homo sapiens Human MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQIVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPVPGFEELKDETSAEPATD fnta_human Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha CAAX farnesyltransferase subunit alpha Ras proteins prenyltransferase subunit alpha FTase-alpha Type I protein geranyl-geranyltransferase subunit alpha FNTA protein protein human Homo sapiens Human MAATEGVGEAAQGGEPGQPAQPPPQPHPPPPQQQHKEEMAAEAGEAVASPMDDGFVSLDSPSYVLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLRDPSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQRYFVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLLDLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIGRSLQSKHSTENDSPTNVQQ fnta-fntb-3 Co-crystal structure of human farnesyltransferase with farnesyldiphosphate and inhibitor compound 66 99867 N/A 99868 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 99869 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 80.500%, free 78.100% 2A fnta-fntb-4 Co-crystal structure of human farnesyltransferase with farnesyldiphosphate and inhibitor compound 49 99867 N/A 99868 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 99869 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 81.600%, free 79.800% 1.8A