eF-site ID 1qfe-B PDB Code 1qfe Chain B click to enlarge Title THE STRUCTURE OF TYPE I 3-DEHYDROQUINATE DEHYDRATASE FROM SALMONELLA TYPHI Classification LYASE Compound PROTEIN (3-DEHYDROQUINATE DEHYDRATASE) Source ORGANISM_SCIENTIFIC: Salmonella typhi; Sequence B:  MKTVTVKNLIIGEGMPKIIVSLMGRDINSVKAEALAYREA TFDILEWRVDHFMDIASTQSVLTAARVIRDAMPDIPLLFT FRSAKEGGEQTITTQHYLTLNRAAIDSGLVDMIDLELFTG DADVKATVDYAHAHNVYVVMSNHDFHQTPSAEEMVSRLRK MQALGADIPKIAVMPQSKHDVLTLLTATLEMQQHYADRPV ITMSMAKEGVISRLAGEVFGSAATFGAVKQASAPGQIAVN DLRSVLMILHNA Description Functional site 1) chain B residue 21 type sequence S description BINDING SITE FOR RESIDUE DHS B 301 source : AC2 2) chain B residue 46 type sequence E description BINDING SITE FOR RESIDUE DHS B 301 source : AC2 3) chain B residue 48 type sequence R description BINDING SITE FOR RESIDUE DHS B 301 source : AC2 4) chain B residue 82 type sequence R description BINDING SITE FOR RESIDUE DHS B 301 source : AC2 5) chain B residue 143 type sequence H description BINDING SITE FOR RESIDUE DHS B 301 source : AC2 6) chain B residue 170 type sequence K description BINDING SITE FOR RESIDUE DHS B 301 source : AC2 7) chain B residue 203 type sequence M description BINDING SITE FOR RESIDUE DHS B 301 source : AC2 8) chain B residue 213 type sequence R description BINDING SITE FOR RESIDUE DHS B 301 source : AC2 9) chain B residue 225 type sequence F description BINDING SITE FOR RESIDUE DHS B 301 source : AC2 10) chain B residue 232 type sequence S description BINDING SITE FOR RESIDUE DHS B 301 source : AC2 11) chain B residue 233 type sequence A description BINDING SITE FOR RESIDUE DHS B 301 source : AC2 12) chain B residue 236 type sequence Q description BINDING SITE FOR RESIDUE DHS B 301 source : AC2 13) chain B residue 86 type catalytic sequence E description 54 source MCSA : MCSA2 14) chain B residue 143 type catalytic sequence H description 54 source MCSA : MCSA2 15) chain B residue 170 type catalytic sequence K description 54 source MCSA : MCSA2 16) chain B residue 143 type ACT_SITE sequence H description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000305|PubMed:24957267 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 170 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 21 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491 source Swiss-Prot : SWS_FT_FI3 19) chain B residue 232 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491 source Swiss-Prot : SWS_FT_FI3 20) chain B residue 46 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491, ECO:0000269|PubMed:24957267 source Swiss-Prot : SWS_FT_FI4 21) chain B residue 213 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491, ECO:0000269|PubMed:24957267 source Swiss-Prot : SWS_FT_FI4 22) chain B residue 236 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491, ECO:0000269|PubMed:24957267 source Swiss-Prot : SWS_FT_FI4 23) chain B residue 82 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352 source Swiss-Prot : SWS_FT_FI5

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