eF-site ID 1hvy-C PDB Code 1hvy Chain C 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 Homo sapiens (Human) (TYSY_HUMAN) Sequence C:  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 C residue 50 type sequence R description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 12) chain C residue 195 type sequence C description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 13) chain C residue 196 type sequence H description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 14) chain C residue 214 type sequence Q description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 15) chain C residue 215 type sequence R description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 16) chain C residue 216 type sequence S description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 17) chain C residue 217 type sequence G description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 18) chain C residue 218 type sequence D description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 19) chain C residue 226 type sequence N description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 20) chain C residue 256 type sequence H description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 21) chain C residue 258 type sequence Y description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 22) chain C residue 175 type sequence R description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 23) chain C residue 176 type sequence R description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 24) chain C residue 163 type sequence R description BINDING SITE FOR RESIDUE BME C 1516 source : BC2 25) chain C residue 167 type sequence T description BINDING SITE FOR RESIDUE BME C 1516 source : BC2 26) chain C residue 178 type sequence I description BINDING SITE FOR RESIDUE BME C 1516 source : BC2 27) chain C residue 196 type ACT_SITE sequence H description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 28) chain C residue 51 type BINDING sequence T description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 29) chain C residue 227 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 30) chain C residue 176 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 31) chain C residue 196 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 32) chain C residue 216 type BINDING sequence S description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 33) chain C residue 257 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 34) chain C residue 219 type BINDING sequence M description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 35) chain C residue 313 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 36) 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 37) 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 38) 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 39) 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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