eF-site ID 1hvy-A PDB Code 1hvy Chain A 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 A:  PPHGELQYLGQIQHILRXGVRKDDRTGTGTLSVFGMQARY SLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKG VKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAE YRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPR DLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPF NIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPL KIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHP TIKMEMAV Description Functional site 1) chain A residue 80 type sequence F description BINDING SITE FOR RESIDUE D16 A 414 source : AC1 2) chain A residue 87 type sequence E description BINDING SITE FOR RESIDUE D16 A 414 source : AC1 3) chain A residue 108 type sequence I description BINDING SITE FOR RESIDUE D16 A 414 source : AC1 4) chain A residue 109 type sequence W description BINDING SITE FOR RESIDUE D16 A 414 source : AC1 5) chain A residue 218 type sequence D description BINDING SITE FOR RESIDUE D16 A 414 source : AC1 6) chain A residue 221 type sequence L description BINDING SITE FOR RESIDUE D16 A 414 source : AC1 7) chain A residue 222 type sequence G description BINDING SITE FOR RESIDUE D16 A 414 source : AC1 8) chain A residue 225 type sequence F description BINDING SITE FOR RESIDUE D16 A 414 source : AC1 9) chain A residue 258 type sequence Y description BINDING SITE FOR RESIDUE D16 A 414 source : AC1 10) chain A residue 311 type sequence M description BINDING SITE FOR RESIDUE D16 A 414 source : AC1 11) chain A residue 312 type sequence A description BINDING SITE FOR RESIDUE D16 A 414 source : AC1 12) chain A residue 50 type sequence R description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 13) chain A residue 192 type sequence L description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 14) chain A residue 195 type sequence C description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 15) chain A residue 196 type sequence H description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 16) chain A residue 214 type sequence Q description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 17) chain A residue 215 type sequence R description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 18) chain A residue 216 type sequence S description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 19) chain A residue 217 type sequence G description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 20) chain A residue 218 type sequence D description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 21) chain A residue 226 type sequence N description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 22) chain A residue 256 type sequence H description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 23) chain A residue 258 type sequence Y description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 24) chain A residue 175 type sequence R description BINDING SITE FOR RESIDUE UMP B 315 source : AC6 25) chain A residue 176 type sequence R description BINDING SITE FOR RESIDUE UMP B 315 source : AC6 26) chain A residue 163 type sequence R description BINDING SITE FOR RESIDUE BME A 1514 source : AC9 27) chain A residue 164 type sequence V description BINDING SITE FOR RESIDUE BME A 1514 source : AC9 28) chain A residue 167 type sequence T description BINDING SITE FOR RESIDUE BME A 1514 source : AC9 29) chain A residue 176 type sequence R description BINDING SITE FOR RESIDUE BME A 1514 source : AC9 30) chain A residue 178 type sequence I description BINDING SITE FOR RESIDUE BME A 1514 source : AC9 31) chain A residue 175-203 type prosite sequence RRIIMCAWNPRDLPLMALPPCHALCQFYV description THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriImcaWNprdlplma.....LpPCHalcQFyV source prosite : PS00091 32) chain A residue 196 type ACT_SITE sequence H description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 51 type BINDING sequence T description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 227 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 176 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 36) chain A residue 196 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 37) chain A residue 216 type BINDING sequence S description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 38) chain A residue 257 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 39) chain A residue 219 type BINDING sequence M description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 40) chain A residue 313 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 41) chain A 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 A 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 A 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 A 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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