eF-site ID 1hvy-CD PDB Code 1hvy Chain C, D click to enlarge Title Human thymidylate synthase complexed with dUMP and Raltitrexed, an antifolate drug, is in the closed conformation Classification TRANSFERASE Compound THYMIDYLATE SYNTHASE Source null (TYSY_HUMAN) Sequence C:  PPHGELQYLGQIQHILRXGVRKDDRTGTGTLSVFGMQARY SLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKG VKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAE YRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPR DLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPF NIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPL KIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHP TIKMEMAV D:  PPHGELQYLGQIQHILRXGVRKDDRTGTGTLSVFGMQARY SLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKG VKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAE YRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPR DLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPF NIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPL KIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHP TIKMEMAV Description Functional site 1) chain C residue 80 type sequence F description BINDING SITE FOR RESIDUE D16 C 416 source : AC3 2) chain C residue 87 type sequence E description BINDING SITE FOR RESIDUE D16 C 416 source : AC3 3) chain C residue 108 type sequence I description BINDING SITE FOR RESIDUE D16 C 416 source : AC3 4) chain C residue 109 type sequence W description BINDING SITE FOR RESIDUE D16 C 416 source : AC3 5) chain C residue 218 type sequence D description BINDING SITE FOR RESIDUE D16 C 416 source : AC3 6) chain C residue 221 type sequence L description BINDING SITE FOR RESIDUE D16 C 416 source : AC3 7) chain C residue 222 type sequence G description BINDING SITE FOR RESIDUE D16 C 416 source : AC3 8) chain C residue 225 type sequence F description BINDING SITE FOR RESIDUE D16 C 416 source : AC3 9) chain C residue 258 type sequence Y description BINDING SITE FOR RESIDUE D16 C 416 source : AC3 10) chain C residue 311 type sequence M description BINDING SITE FOR RESIDUE D16 C 416 source : AC3 11) chain D residue 80 type sequence F description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 12) chain D residue 87 type sequence E description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 13) chain D residue 108 type sequence I description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 14) chain D residue 109 type sequence W description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 15) chain D residue 112 type sequence N description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 16) chain D residue 218 type sequence D description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 17) chain D residue 221 type sequence L description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 18) chain D residue 222 type sequence G description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 19) chain D residue 225 type sequence F description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 20) chain D residue 258 type sequence Y description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 21) chain D residue 311 type sequence M description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 22) chain D residue 312 type sequence A description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 23) chain C residue 50 type sequence R description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 24) chain C residue 195 type sequence C description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 25) chain C residue 196 type sequence H description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 26) chain C residue 214 type sequence Q description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 27) chain C residue 215 type sequence R description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 28) chain C residue 216 type sequence S description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 29) chain C residue 217 type sequence G description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 30) chain C residue 218 type sequence D description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 31) chain C residue 226 type sequence N description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 32) chain C residue 256 type sequence H description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 33) chain C residue 258 type sequence Y description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 34) chain D residue 175 type sequence R description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 35) chain D residue 176 type sequence R description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 36) chain C residue 175 type sequence R description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 37) chain C residue 176 type sequence R description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 38) chain D residue 50 type sequence R description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 39) chain D residue 135 type sequence Y description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 40) chain D residue 195 type sequence C description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 41) chain D residue 196 type sequence H description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 42) chain D residue 214 type sequence Q description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 43) chain D residue 215 type sequence R description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 44) chain D residue 216 type sequence S description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 45) chain D residue 217 type sequence G description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 46) chain D residue 218 type sequence D description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 47) chain D residue 226 type sequence N description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 48) chain D residue 256 type sequence H description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 49) chain D residue 258 type sequence Y description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 50) chain C residue 163 type sequence R description BINDING SITE FOR RESIDUE BME C 1516 source : BC2 51) chain C residue 167 type sequence T description BINDING SITE FOR RESIDUE BME C 1516 source : BC2 52) chain C residue 178 type sequence I description BINDING SITE FOR RESIDUE BME C 1516 source : BC2 53) chain D residue 163 type sequence R description BINDING SITE FOR RESIDUE BME D 1517 source : BC3 54) chain D residue 167 type sequence T description BINDING SITE FOR RESIDUE BME D 1517 source : BC3 55) chain D residue 174 type sequence D description BINDING SITE FOR RESIDUE BME D 1517 source : BC3 56) chain D residue 176 type sequence R description BINDING SITE FOR RESIDUE BME D 1517 source : BC3 57) chain D residue 178 type sequence I description BINDING SITE FOR RESIDUE BME D 1517 source : BC3 58) chain C residue 196 type ACT_SITE sequence H description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 59) chain D residue 196 type ACT_SITE sequence H description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 60) chain C residue 51 type BINDING sequence T description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 61) chain C residue 227 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 62) chain D residue 51 type BINDING sequence T description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 63) chain D residue 227 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 64) chain C residue 176 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 65) chain D residue 176 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 66) chain D residue 196 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 67) chain D residue 216 type BINDING sequence S description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 68) chain D residue 257 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 69) chain C residue 196 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 70) chain C residue 216 type BINDING sequence S description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 71) chain C residue 257 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 72) chain C residue 219 type BINDING sequence M description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 73) chain C residue 313 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 74) chain D residue 219 type BINDING sequence M description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 75) chain D residue 313 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 76) chain C residue 115 type MOD_RES sequence R description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 77) chain D residue 115 type MOD_RES sequence R description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 78) chain C residue 293 type CROSSLNK sequence A description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 79) chain C residue 309 type CROSSLNK sequence M description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 80) chain D residue 288 type CROSSLNK sequence I description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 81) chain D residue 293 type CROSSLNK sequence A description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 82) chain D residue 309 type CROSSLNK sequence M description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 83) chain C residue 288 type CROSSLNK sequence I description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7

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