eF-site ID 1fur-AB PDB Code 1fur Chain A, B click to enlarge Title FUMARASE MUTANT H188N WITH BOUND SUBSTRATE L-MALATE AT PUTATIVE ACTIVATOR SITE Classification HYDROLYASE Compound FUMARASE C Source null (FUMC_ECOLI) Sequence A:  VRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTS LIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVLAG QHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRG MERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQLIPQ LKTLTQTLNEKSRAFADIVKIGRTNLQDATPLTLGQEISG WVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYA RRVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKG LAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPG KVNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRP MVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLN ESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALG YLSEAEFDSWVRPEQM B:  MNTVRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKM PTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEV LAGQHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGG VRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQL IPQLKTLTQTLNEKSRAFADIVKIGRTNLQDATPLTLGQE ISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHP EYARRVADELAVITCAPFVTAPNKFEALATCDALVQAHGA LKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPMPGK VNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPM VIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLNE SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGY LSEAEFDSWVRPEQM Description Functional site 1) chain B residue 98 type sequence S description THE ACTIVE SITE IS GENERATED FROM THREE OF THE FOUR SUBUNITS WITHIN THE TETRAMER. THE ENTRY CONTAINS CHAINS A AND B. CHAINS C AND D CAN BE GENERATED FROM CHAINS A AND B. THE ACTIVE SITE CONTAINS RESIDUES FROM CHAINS B, C, AND D. BECAUSE OF PDB FORMAT RESTRICTIONS, ONLY THE RESIDUES FROM CHAIN B ARE LISTED ON THE SITE RECORD BELOW. THE FOLLOWING RESIDUES ARE ALSO PART OF THE ACTIVE SITE: LYS C 324 ASN C 326 GLU C 331 ASN D 188 source : S1 2) chain B residue 100 type sequence T description THE ACTIVE SITE IS GENERATED FROM THREE OF THE FOUR SUBUNITS WITHIN THE TETRAMER. THE ENTRY CONTAINS CHAINS A AND B. CHAINS C AND D CAN BE GENERATED FROM CHAINS A AND B. THE ACTIVE SITE CONTAINS RESIDUES FROM CHAINS B, C, AND D. BECAUSE OF PDB FORMAT RESTRICTIONS, ONLY THE RESIDUES FROM CHAIN B ARE LISTED ON THE SITE RECORD BELOW. THE FOLLOWING RESIDUES ARE ALSO PART OF THE ACTIVE SITE: LYS C 324 ASN C 326 GLU C 331 ASN D 188 source : S1 3) chain B residue 141 type sequence N description THE ACTIVE SITE IS GENERATED FROM THREE OF THE FOUR SUBUNITS WITHIN THE TETRAMER. THE ENTRY CONTAINS CHAINS A AND B. CHAINS C AND D CAN BE GENERATED FROM CHAINS A AND B. THE ACTIVE SITE CONTAINS RESIDUES FROM CHAINS B, C, AND D. BECAUSE OF PDB FORMAT RESTRICTIONS, ONLY THE RESIDUES FROM CHAIN B ARE LISTED ON THE SITE RECORD BELOW. THE FOLLOWING RESIDUES ARE ALSO PART OF THE ACTIVE SITE: LYS C 324 ASN C 326 GLU C 331 ASN D 188 source : S1 4) chain A residue 126 type sequence R description BINDING SITE FOR RESIDUE MLT A 468 source : AC1 5) chain A residue 129 type sequence H description BINDING SITE FOR RESIDUE MLT A 468 source : AC1 6) chain A residue 130 type sequence P description BINDING SITE FOR RESIDUE MLT A 468 source : AC1 7) chain A residue 131 type sequence N description BINDING SITE FOR RESIDUE MLT A 468 source : AC1 8) chain A residue 132 type sequence D description BINDING SITE FOR RESIDUE MLT A 468 source : AC1 9) chain B residue 124 type sequence M description BINDING SITE FOR RESIDUE MLT B 468 source : AC2 10) chain B residue 126 type sequence R description BINDING SITE FOR RESIDUE MLT B 468 source : AC2 11) chain B residue 129 type sequence H description BINDING SITE FOR RESIDUE MLT B 468 source : AC2 12) chain B residue 130 type sequence P description BINDING SITE FOR RESIDUE MLT B 468 source : AC2 13) chain B residue 131 type sequence N description BINDING SITE FOR RESIDUE MLT B 468 source : AC2 14) chain B residue 132 type sequence D description BINDING SITE FOR RESIDUE MLT B 468 source : AC2 15) chain A residue 188 type catalytic sequence N description 569 source MCSA : MCSA1 16) chain A residue 318 type catalytic sequence S description 569 source MCSA : MCSA1 17) chain A residue 324 type catalytic sequence K description 569 source MCSA : MCSA1 18) chain A residue 331 type catalytic sequence E description 569 source MCSA : MCSA1 19) chain B residue 188 type catalytic sequence N description 569 source MCSA : MCSA2 20) chain B residue 324 type catalytic sequence K description 569 source MCSA : MCSA2 21) chain B residue 331 type catalytic sequence E description 569 source MCSA : MCSA2 22) chain A 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 23) 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 24) chain B residue 188 type ACT_SITE sequence N description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:9098893 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 188 type ACT_SITE sequence N description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:9098893 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 318 type ACT_SITE sequence S description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00743 source Swiss-Prot : SWS_FT_FI2 27) 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 28) chain A 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 29) chain A 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 30) 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 31) chain A residue 317-326 type prosite sequence GSSIMPGKVN description FUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN source prosite : PS00163 32) chain A 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 33) 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 34) chain A residue 187 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00743 source Swiss-Prot : SWS_FT_FI7 35) chain A residue 319 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00743 source Swiss-Prot : SWS_FT_FI7 36) chain A residue 324 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00743 source Swiss-Prot : SWS_FT_FI7 37) chain B residue 187 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00743 source Swiss-Prot : SWS_FT_FI7 38) chain B residue 324 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00743 source Swiss-Prot : SWS_FT_FI7 39) chain A 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 40) 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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