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/ http://www.ebi.ac.uk/ yang-2004c-1 Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases. 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 Biochemistry (0006-2960) 2004 Only protein-protein interactions imex curation 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 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. hppd_rat 4-hydroxyphenylpyruvate dioxygenase Hpd 4-hydroxyphenylpyruvic acid oxidase F Alloantigen protein protein rat Rattus norvegicus (Rat) Rat MTTYSNKGPKPERGRFLHFHSVTFWVGNAKQAASFYCNKMGFEPLAYKGLETGSREVVSHVIKQGKIVFVLCSALNPWNKEMGDHLVKHGDGVKDIAFEVEDCEHIVQKARERGAKIVREPWVEEDKFGKVKFAVLQTYGDTTHTLVEKINYTGRFLPGFEAPTYKDTLLPKLPSCNLEIIDHIVGNQPDQEMESASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVANYEESIKMPINEPAPGRKKSQIQEYVDYNGGAGVQHIALRTEDIITTIRHLRERGMEFLAVPSSYYRLLRENLKTSKIQVKENMDVLEELKILVDYDEKGYLLQIFTKPMQDRPTLFLEVIQRHNHQGFGAGNFNSLFKAFEEEQALRGNLTDLETNGVRSGM 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. hpd Structural analysis reveals Arabidopsis 4-hydroxyphenylpyruvate dioxygenase is homodimeric. 608258 N/A 608259 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 Stoichiometry: 2.0 direct interaction direct interaction false false false 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 protein was trucated by removal of 21 amino acids from the N terminus of the protein. hpd-3 Structural analysis reveals Arabidopsis 4-hydroxyphenylpyruvate dioxygenase is homodimeric and binds DAS869 608258 N/A 608259 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 phe360 Phe 360 binds DAS869 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false phe430 Phe 430 binds DAS869 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 2.0 N/A 608260 unspecified role unspecified role neutral component neutral component direct interaction direct interaction false false false 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 protein was trucated by removal of 21 amino acids from the N terminus of the protein. hpd-4 Structural analysis reveals Rat 4-hydroxyphenylpyruvate dioxygenase is homodimeric. 608258 N/A 608260 unspecified role unspecified role neutral component neutral component N/A 608261 unspecified role unspecified role neutral component neutral component Stoichiometry: 2.0 direct interaction direct interaction false false false 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 hpd-5 Structural analysis reveals Arabidopsis 4-hydroxyphenylpyruvate dioxygenase is homodimeric and binds DAS645 608258 N/A 608259 unspecified role unspecified role neutral component neutral component Stoichiometry: 2.0 N/A 608262 unspecified role unspecified role neutral component neutral component direct interaction direct interaction false false false Working R factor = 18.8 . Free R factor = 23.4 1.9 Angstroms. Table 1 Figure 7 The HPPD protein was truncated by 21 N terminal amino acids