eF-site ID 1fuq-B PDB Code 1fuq Chain B click to enlarge Title FUMARASE WITH BOUND 3-TRIMETHYLSILYLSUCCINIC ACID Classification LYASE Compound FUMARASE C Source Escherichia coli (strain K12) (FUMC_ECOLI) Sequence B:  MNTVRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKM PTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEV LAGQHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGG VRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQL IPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQE ISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHP EYARRVADELAVITCAPFVTAPNKFEALATCDALVQAHGA LKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPMPGK VNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPM VIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLNE SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGY LSEAEFDSWVRPEQM Description Functional site 1) chain B residue 187 type sequence T description BINDING SITE FOR RESIDUE CIT A 1001 source : AC2 2) chain B residue 188 type sequence H description BINDING SITE FOR RESIDUE CIT A 1001 source : AC2 3) chain B residue 126 type sequence R description BINDING SITE FOR RESIDUE SIF B 1001 source : AC3 4) chain B residue 129 type sequence H description BINDING SITE FOR RESIDUE SIF B 1001 source : AC3 5) chain B residue 130 type sequence P description BINDING SITE FOR RESIDUE SIF B 1001 source : AC3 6) chain B residue 131 type sequence N description BINDING SITE FOR RESIDUE SIF B 1001 source : AC3 7) chain B residue 132 type sequence D description BINDING SITE FOR RESIDUE SIF B 1001 source : AC3 8) chain B residue 100 type sequence T description BINDING SITE FOR RESIDUE CIT B 1002 source : AC4 9) chain B residue 139 type sequence S description BINDING SITE FOR RESIDUE CIT B 1002 source : AC4 10) chain B residue 140 type sequence S description BINDING SITE FOR RESIDUE CIT B 1002 source : AC4 11) chain B residue 141 type sequence N description BINDING SITE FOR RESIDUE CIT B 1002 source : AC4 12) chain B residue 324 type sequence K description BINDING SITE FOR RESIDUE CIT B 1002 source : AC4 13) chain B residue 326 type sequence N description BINDING SITE FOR RESIDUE CIT B 1002 source : AC4 14) chain B residue 188 type catalytic sequence H description 569 source MCSA : MCSA2 15) chain B residue 324 type catalytic sequence K description 569 source MCSA : MCSA2 16) chain B residue 331 type catalytic sequence E description 569 source MCSA : MCSA2 17) chain B residue 98 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:12021453, ECO:0000305|PubMed:8909293, ECO:0000305|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1KQ7, ECO:0007744|PDB:2FUS source Swiss-Prot : SWS_FT_FI3 18) chain B residue 126 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1FUR source Swiss-Prot : SWS_FT_FI4 19) chain B residue 188 type ACT_SITE sequence H description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:9098893 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 129 type BINDING sequence H description in site B => ECO:0000269|PubMed:12021453, ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1FUR, ECO:0007744|PDB:1KQ7 source Swiss-Prot : SWS_FT_FI5 21) chain B residue 139 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:12021453, ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1KQ7, ECO:0007744|PDB:2FUS source Swiss-Prot : SWS_FT_FI6 22) chain B residue 187 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00743 source Swiss-Prot : SWS_FT_FI7 23) chain B residue 324 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00743 source Swiss-Prot : SWS_FT_FI7 24) chain B residue 331 type SITE sequence E description Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:8909293 source Swiss-Prot : SWS_FT_FI8

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