IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases. Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases. Biochemistry (0006-2960) 2004 imex curation Yang C., Pflugrath JW., Camper DL., Foster ML., Pernich DJ., Walsh TA. tawalsh@dow.com 29-OCT-2007: Contacted by JYOTI. orchard Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Yang C., Pflugrath JW., Camper DL., Foster ML., Pernich DJ., Walsh TA. tawalsh@dow.com Accepted 2007-JUL-7 by ORCHARD. Biochemistry (0006-2960) 2004 orchard Only protein-protein interactions imex curation hppd_rat 4-hydroxyphenylpyruvate dioxygenase Hpd 4-hydroxyphenylpyruvic acid oxidase F Alloantigen protein protein rat Rattus norvegicus (Rat) Rat MTTYSNKGPKPERGRFLHFHSVTFWVGNAKQAASFYCNKMGFEPLAYKGLETGSREVVSHVIKQGKIVFVLCSALNPWNKEMGDHLVKHGDGVKDIAFEVEDCEHIVQKARERGAKIVREPWVEEDKFGKVKFAVLQTYGDTTHTLVEKINYTGRFLPGFEAPTYKDTLLPKLPSCNLEIIDHIVGNQPDQEMESASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVANYEESIKMPINEPAPGRKKSQIQEYVDYNGGAGVQHIALRTEDIITTIRHLRERGMEFLAVPSSYYRLLRENLKTSKIQVKENMDVLEELKILVDYDEKGYLLQIFTKPMQDRPTLFLEVIQRHNHQGFGAGNFNSLFKAFEEEQALRGNLTDLETNGVRSGM E8D1B7B9FC4C0EC3 das645 [1-tert-butyl-3-(2,4-dichlorophenyl)-5-hydroxy-1h-pyrazol-4-yl][2-chloro-4-(methylsulfonyl)phenyl]methanone small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) Experimental herbicides from the Dow AgroSciences collection. Experimental herbicides from the Dow AgroSciences collection. hppd_arath 4-hydroxyphenylpyruvate dioxygenase HPD 4-hydroxyphenylpyruvic acid oxidase PDS1 F12K11.9 At1g06570 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MGHQNAAVSENQNHDDGAASSPGFKLVGFSKFVRKNPKSDKFKVKRFHHIEFWCGDATNVARRFSWGLGMRFSAKSDLSTGNMVHASYLLTSGDLRFLFTAPYSPSLSAGEIKPTTTASIPSFDHGSCRSFFSSHGLGVRAVAIEVEDAESAFSISVANGAIPSSPPIVLNEAVTIAEVKLYGDVVLRYVSYKAEDTEKSEFLPGFERVEDASSFPLDYGIRRLDHAVGNVPELGPALTYVAGFTGFHQFAEFTADDVGTAESGLNSAVLASNDEMVLLPINEPVHGTKRKSQIQTYLEHNEGAGLQHLALMSEDIFRTLREMRKRSSIGGFDFMPSPPPTYYQNLKKRVGDVLSDDQIKECEELGILVDRDDQGTLLQIFTKPLGDRPTIFIEIIQRVGCMMKDEEGKAYQSGGCGGFGKGNFSELFKSIEEYEKTLEAKQLVG FD0442F93556B3F5 das869 (1-tert-butyl-5-hydroxy-1h-pyrazol-4-yl){6-[dihydroxy(methyl)-lambda~4~-sulfanyl]-4'-methoxy-2-methyl-1,1'-biphenyl-3-yl}methanone small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) Experimental herbicides from the Dow AgroSciences collection. Experimental herbicides from the Dow AgroSciences collection. hpd 1 4 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 direct interaction direct interaction Working R factor = 21.6 . Free R factor = 26.6. 1.8 Angstroms. The protein complex was homodimeric. It was not possible to distinguish between colbalt and iron ions within the protein structure , the active site metal ion cofactor is therefore referred to as 'M' by the authors. The metal ion in the AtHPPD structure is coordinated by His205, His287 Glu373, and three water molecules forming an octahedral complex within the homodimer. Table 1 Figure 2a The truncated AtHPPD was overexpressed in E. coli and purified to homogeneity. The structure of the purified enzyme was solved by multiple isomorphous replacement and refined to 1.8 A (Table 1). The enzyme forms a homodimer The protein was trucated by removal of 21 amino acids from the N terminus of the protein. hpd-3 1 4 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 phe360 Phe 360 binds DAS869 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain phe430 Phe 430 binds DAS869 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 5 unspecified role unspecified role neutral component neutral component direct interaction direct interaction Working R factor = 21.6 . Free R factor = 26.6. 1.8 Angstroms. The protein complex was homodimeric. It was not possible to distinguish between colbalt and iron ions within the protein structure , the active site metal ion cofactor is therefore referred to as 'M' by the authors. The metal ion in the AtHPPD structure is coordinated by His205, His287 Glu373, and one water molecule and a 1,3-diketone moiety of the DAS869 inhibitor forming an octahedral complex within the homodimer. Table 1 Figure 2a The truncated AtHPPD was overexpressed in E. coli and purified to homogeneity. The structure of the purified enzyme was solved by multiple isomorphous replacement and refined to 1.8 A(Table 1). The enzyme forms a homodimer The protein was trucated by removal of 21 amino acids from the N terminus of the protein. hpd-4 1 5 unspecified role unspecified role neutral component neutral component 2 unspecified role unspecified role neutral component neutral component direct interaction direct interaction Working R factor = 21.6 . Free R factor = 27.1 2.15 Angstroms. The protein complex was homodimeric. It was not possible to distinguish between colbalt and iron ions within the protein structure , the active site metal ion cofactor is therefore referred to as 'M' by the authors. The metal ion in the AtHPPD structure is coordinated by His183, His266 Glu349, and one water molecule and a 1,3-diketone moiety of the DAS869 inhibitor forming an octahedral complex within the homodimer. Table 1 Figure 3 the HPPD from rat (RnHPPD) was cloned, overexpressed in E. coli, purified,and cocrystallized with DAS869 hpd-5 1 4 unspecified role unspecified role neutral component neutral component 3 unspecified role unspecified role neutral component neutral component direct interaction direct interaction Working R factor = 18.8 . Free R factor = 23.4 1.9 Angstroms. Table 1 Figure 7 The structure of DAS645 in complex with AtHPPD (AtHPPD- 645) was solved and refined to 1.9 � resolution. The HPPD protein was truncated by 21 N terminal amino acids