eF-site ID 1hvy-D PDB Code 1hvy Chain 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 Homo sapiens (Human) (TYSY_HUMAN) Sequence D:  PPHGELQYLGQIQHILRXGVRKDDRTGTGTLSVFGMQARY SLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKG VKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAE YRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPR DLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPF NIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPL KIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHP TIKMEMAV Description Functional site 1) chain D residue 80 type sequence F description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 2) chain D residue 87 type sequence E description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 3) chain D residue 108 type sequence I description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 4) chain D residue 109 type sequence W description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 5) chain D residue 112 type sequence N description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 6) chain D residue 218 type sequence D description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 7) chain D residue 221 type sequence L description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 8) chain D residue 222 type sequence G description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 9) chain D residue 225 type sequence F description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 10) chain D residue 258 type sequence Y description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 11) chain D residue 311 type sequence M description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 12) chain D residue 312 type sequence A description BINDING SITE FOR RESIDUE D16 D 417 source : AC4 13) chain D residue 175 type sequence R description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 14) chain D residue 176 type sequence R description BINDING SITE FOR RESIDUE UMP C 316 source : AC7 15) chain D residue 50 type sequence R description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 16) chain D residue 135 type sequence Y description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 17) chain D residue 195 type sequence C description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 18) chain D residue 196 type sequence H description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 19) chain D residue 214 type sequence Q description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 20) chain D residue 215 type sequence R description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 21) chain D residue 216 type sequence S description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 22) chain D residue 217 type sequence G description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 23) chain D residue 218 type sequence D description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 24) chain D residue 226 type sequence N description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 25) chain D residue 256 type sequence H description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 26) chain D residue 258 type sequence Y description BINDING SITE FOR RESIDUE UMP D 317 source : AC8 27) chain D residue 163 type sequence R description BINDING SITE FOR RESIDUE BME D 1517 source : BC3 28) chain D residue 167 type sequence T description BINDING SITE FOR RESIDUE BME D 1517 source : BC3 29) chain D residue 174 type sequence D description BINDING SITE FOR RESIDUE BME D 1517 source : BC3 30) chain D residue 176 type sequence R description BINDING SITE FOR RESIDUE BME D 1517 source : BC3 31) chain D residue 178 type sequence I description BINDING SITE FOR RESIDUE BME D 1517 source : BC3 32) chain D residue 196 type ACT_SITE sequence H description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 33) chain D residue 51 type BINDING sequence T description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 34) chain D residue 227 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 35) chain D residue 176 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 36) chain D residue 196 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 37) chain D residue 216 type BINDING sequence S description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 38) chain D residue 257 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 39) chain D residue 219 type BINDING sequence M description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 40) chain D residue 313 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 41) 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 42) 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 43) 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 44) 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

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