eF-site ID 1fur-B PDB Code 1fur Chain B click to enlarge Title FUMARASE MUTANT H188N WITH BOUND SUBSTRATE L-MALATE AT PUTATIVE ACTIVATOR SITE Classification HYDROLYASE Compound FUMARASE C Source Escherichia coli (strain K12) (FUMC_ECOLI) Sequence 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 B residue 124 type sequence M description BINDING SITE FOR RESIDUE MLT B 468 source : AC2 5) chain B residue 126 type sequence R description BINDING SITE FOR RESIDUE MLT B 468 source : AC2 6) chain B residue 129 type sequence H description BINDING SITE FOR RESIDUE MLT B 468 source : AC2 7) chain B residue 130 type sequence P description BINDING SITE FOR RESIDUE MLT B 468 source : AC2 8) chain B residue 131 type sequence N description BINDING SITE FOR RESIDUE MLT B 468 source : AC2 9) chain B residue 132 type sequence D description BINDING SITE FOR RESIDUE MLT B 468 source : AC2 10) chain B residue 188 type catalytic sequence N description 569 source MCSA : MCSA2 11) chain B residue 324 type catalytic sequence K description 569 source MCSA : MCSA2 12) chain B residue 331 type catalytic sequence E description 569 source MCSA : MCSA2 13) 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 14) 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 15) 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 16) 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 17) chain B residue 187 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00743 source Swiss-Prot : SWS_FT_FI7 18) chain B residue 324 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00743 source Swiss-Prot : SWS_FT_FI7 19) 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 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

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