eF-site ID 6syp-.AAA PDB Code 6syp Chain AAA click to enlarge Title Human DHODH bound to inhibitor IPP/CNRS-A017 Classification OXIDOREDUCTASE Compound Dihydroorotate dehydrogenase Source (PYRD_HUMAN) Sequence AAA:  LDPESAHRLAVRFTSLGLLPRARFQDSDMLEVRVLGHKFR NPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGN PRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQA KLTEDGLPLGVNLGKNKTSVDAAEDYAEGVRVLGPLADYL VVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRRVHR PAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSR PAGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVP IIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGK VKRELEALLKEQGFGGVTDAIGADHRR Description Functional site 1) chain AAA residue 114-133 type prosite sequence GFVEIGSVTPKPQEGNPRPR description DHODEHASE_1 Dihydroorotate dehydrogenase signature 1. GfveiGSVTpkpQeGNprPR source prosite : PS00911 2) chain AAA residue 330-350 type prosite sequence IIGVGGVSSGQDALEKIRAGA description DHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIGvGGVsSgqdAleKIrAGA source prosite : PS00912 3) chain AAA residue 145 type catalytic sequence N description 109 source MCSA : MCSA1 4) chain AAA residue 149 type catalytic sequence F description 109 source MCSA : MCSA1 5) chain AAA residue 215 type catalytic sequence S description 109 source MCSA : MCSA1 6) chain AAA residue 217 type catalytic sequence N description 109 source MCSA : MCSA1 7) chain AAA residue 218 type catalytic sequence T description 109 source MCSA : MCSA1 8) chain AAA residue 255 type catalytic sequence K description 109 source MCSA : MCSA1 9) chain AAA residue 284 type catalytic sequence N description 109 source MCSA : MCSA1 10) chain AAA residue 120 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261 source Swiss-Prot : SWS_FT_FI5 11) chain AAA residue 181 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261 source Swiss-Prot : SWS_FT_FI5 12) chain AAA residue 212 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261 source Swiss-Prot : SWS_FT_FI5 13) chain AAA residue 255 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261 source Swiss-Prot : SWS_FT_FI5 14) chain AAA residue 283 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261 source Swiss-Prot : SWS_FT_FI5 15) chain AAA residue 306 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261 source Swiss-Prot : SWS_FT_FI5 16) chain AAA residue 335 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261 source Swiss-Prot : SWS_FT_FI5 17) chain AAA residue 356 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261 source Swiss-Prot : SWS_FT_FI5 18) chain AAA residue 96 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261 source Swiss-Prot : SWS_FT_FI5 19) chain AAA residue 145 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI6 20) chain AAA residue 284 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI6 21) chain AAA residue 100 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI6 22) chain AAA residue 215 type ACT_SITE sequence S description Nucleophile source Swiss-Prot : SWS_FT_FI4

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