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 morollo-2001-1 Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Morollo AA., Eck MJ. PDBe - Data obtained from the Protein Data Bank Europe Nat. Struct. Biol. (1072-8368) 2001 trpe_salty Anthranilate synthase component 1 trpE STM1723 protein protein salty Salmonella typhimurium MQTPKPTLELLTCDAAYRENPTALFHQVCGDRPATLLLESADIDSKDDLKSLLLVDSALRITALGDTVTIQALSDNGASLLPLLDTALPAGVENDVLPAGRVLRFPPVSPLLDEDARLCSLSVFDAFRLLQGVVNIPTQEREAMFFGGLFAYDLVAGFEALPHLEAGNNCPDYCFYLAETLMVIDHQKKSTRIQASLFTASDREKQRLNARLAYLSQQLTQPAPPLPVTPVPDMRCECNQSDDAFGAVVRQLQKAIRAGEIFQVVPSRRFSLPCPSPLAAYYVLKKSNPSPYMFFMQDNDFTLFGASPESSLKYDAASRQIEIYPIAGTRPRGRRADGTLDRDLDSRIELDMRTDHKELSEHLMLVDLARNDLARICTPGSRYVADLTKVDRYSYVMHLVSRVVGELRHDLDALHAYRACMNMGTLSGAPKVRAMQLIADAEGQRRGSYGGAVGYFTAHGDLDTCIVIRSALVENGIATVQAGAGIVLDSVPQSEADETRNKARAVLRAIATAHHAQETF trpgd_salty Bifunctional protein TrpGD trpGD trpD STM1724 protein protein salty Salmonella typhimurium MADILLLDNIDSFTWNLADQLRTNGHNVVIYRNHIPAQTLIDRLATMKNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLVGSNVPAGLTINAHFNGMVMAVRHDADRVCGFQFHPESILTTQGARLLEQTLAWAQQKLEPTNTLQPILEKLYQAQTLTQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFPRPEYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGLRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGGMDEVSLHAPTIVAELHDGEIKSYQLTAEDFGLTPYHQDQLAGGTPEENRDILTRLLQGKGDAAHEAAVAANVAMLMRLHGQEDLKANAQTVLDVLRNGTAYDRVTALAARG trpd-trpe-1 Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium 99683 N/A 99684 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 99685 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 tetrameric, multimeric working 78.100%, free 75.400% 1.9A