eF-site ID 1hvy-AB PDB Code 1hvy Chain A, B 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 A:  PPHGELQYLGQIQHILRXGVRKDDRTGTGTLSVFGMQARY SLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKG VKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAE YRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPR DLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPF NIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPL KIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHP TIKMEMAV B:  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 B residue 87 type sequence E description BINDING SITE FOR RESIDUE D16 B 415 source : AC2 13) chain B residue 108 type sequence I description BINDING SITE FOR RESIDUE D16 B 415 source : AC2 14) chain B residue 109 type sequence W description BINDING SITE FOR RESIDUE D16 B 415 source : AC2 15) chain B residue 112 type sequence N description BINDING SITE FOR RESIDUE D16 B 415 source : AC2 16) chain B residue 218 type sequence D description BINDING SITE FOR RESIDUE D16 B 415 source : AC2 17) chain B residue 221 type sequence L description BINDING SITE FOR RESIDUE D16 B 415 source : AC2 18) chain B residue 222 type sequence G description BINDING SITE FOR RESIDUE D16 B 415 source : AC2 19) chain B residue 225 type sequence F description BINDING SITE FOR RESIDUE D16 B 415 source : AC2 20) chain B residue 258 type sequence Y description BINDING SITE FOR RESIDUE D16 B 415 source : AC2 21) chain B residue 308 type sequence K description BINDING SITE FOR RESIDUE D16 B 415 source : AC2 22) chain B residue 311 type sequence M description BINDING SITE FOR RESIDUE D16 B 415 source : AC2 23) chain B residue 312 type sequence A description BINDING SITE FOR RESIDUE D16 B 415 source : AC2 24) chain A residue 50 type sequence R description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 25) chain A residue 192 type sequence L description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 26) chain A residue 195 type sequence C description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 27) chain A residue 196 type sequence H description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 28) chain A residue 214 type sequence Q description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 29) chain A residue 215 type sequence R description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 30) chain A residue 216 type sequence S description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 31) chain A residue 217 type sequence G description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 32) chain A residue 218 type sequence D description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 33) chain A residue 226 type sequence N description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 34) chain A residue 256 type sequence H description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 35) chain A residue 258 type sequence Y description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 36) chain B residue 175 type sequence R description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 37) chain B residue 176 type sequence R description BINDING SITE FOR RESIDUE UMP A 314 source : AC5 38) chain A residue 175 type sequence R description BINDING SITE FOR RESIDUE UMP B 315 source : AC6 39) chain A residue 176 type sequence R description BINDING SITE FOR RESIDUE UMP B 315 source : AC6 40) chain B residue 50 type sequence R description BINDING SITE FOR RESIDUE UMP B 315 source : AC6 41) chain B residue 192 type sequence L description BINDING SITE FOR RESIDUE UMP B 315 source : AC6 42) chain B residue 195 type sequence C description BINDING SITE FOR RESIDUE UMP B 315 source : AC6 43) chain B residue 196 type sequence H description BINDING SITE FOR RESIDUE UMP B 315 source : AC6 44) chain B residue 214 type sequence Q description BINDING SITE FOR RESIDUE UMP B 315 source : AC6 45) chain B residue 215 type sequence R description BINDING SITE FOR RESIDUE UMP B 315 source : AC6 46) chain B residue 216 type sequence S description BINDING SITE FOR RESIDUE UMP B 315 source : AC6 47) chain B residue 217 type sequence G description BINDING SITE FOR RESIDUE UMP B 315 source : AC6 48) chain B residue 218 type sequence D description BINDING SITE FOR RESIDUE UMP B 315 source : AC6 49) chain B residue 226 type sequence N description BINDING SITE FOR RESIDUE UMP B 315 source : AC6 50) chain B residue 256 type sequence H description BINDING SITE FOR RESIDUE UMP B 315 source : AC6 51) chain B residue 258 type sequence Y description BINDING SITE FOR RESIDUE UMP B 315 source : AC6 52) chain A residue 163 type sequence R description BINDING SITE FOR RESIDUE BME A 1514 source : AC9 53) chain A residue 164 type sequence V description BINDING SITE FOR RESIDUE BME A 1514 source : AC9 54) chain A residue 167 type sequence T description BINDING SITE FOR RESIDUE BME A 1514 source : AC9 55) chain A residue 176 type sequence R description BINDING SITE FOR RESIDUE BME A 1514 source : AC9 56) chain A residue 178 type sequence I description BINDING SITE FOR RESIDUE BME A 1514 source : AC9 57) chain B residue 163 type sequence R description BINDING SITE FOR RESIDUE BME B 1515 source : BC1 58) chain B residue 167 type sequence T description BINDING SITE FOR RESIDUE BME B 1515 source : BC1 59) chain B residue 174 type sequence D description BINDING SITE FOR RESIDUE BME B 1515 source : BC1 60) chain B residue 176 type sequence R description BINDING SITE FOR RESIDUE BME B 1515 source : BC1 61) chain B residue 178 type sequence I description BINDING SITE FOR RESIDUE BME B 1515 source : BC1 62) chain A residue 175-203 type prosite sequence RRIIMCAWNPRDLPLMALPPCHALCQFYV description THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriImcaWNprdlplma.....LpPCHalcQFyV source prosite : PS00091 63) chain A residue 196 type ACT_SITE sequence H description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 64) chain B residue 196 type ACT_SITE sequence H description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 65) chain A residue 51 type BINDING sequence T description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 66) chain A residue 227 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 67) chain B residue 51 type BINDING sequence T description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 68) chain B residue 227 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 69) chain A residue 176 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 70) chain B residue 176 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 71) chain A residue 196 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 72) chain A residue 216 type BINDING sequence S description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 73) chain A residue 257 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 74) chain B residue 196 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 75) chain B residue 216 type BINDING sequence S description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 76) chain B residue 257 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 77) chain A residue 219 type BINDING sequence M description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 78) chain A residue 313 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 79) chain B residue 219 type BINDING sequence M description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 80) chain B residue 313 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 81) 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 82) chain B residue 115 type MOD_RES sequence R description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 83) 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 84) 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 85) 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 86) chain B 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 87) chain B 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 88) chain B 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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