eF-site ID 6oju-ABCD PDB Code 6oju Chain A, B, C, D click to enlarge Title Crystal structure of human thymidylate synthase Delta (7-29) in complex with dUMP and 2-amino-4-oxo-4,7-dihydro-pyrrolo[2,3-d]pyrimidine-methyl-phenyl-D-glutamic acid Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Thymidylate synthase,Thymidylate synthase Source (TYSY_HUMAN) Sequence A:  SELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLR DEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKI WDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRD MESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLP LMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIA SYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQ LQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIK MEMAV B:  SELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLR DEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKI WDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRD MESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLP LMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIA SYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQ LQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIK MEMAV C:  SELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLR DEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKI WDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRD MESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLP LMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIA SYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQ LQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIK MEMAV D:  SELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLR DEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKI WDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRD MESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLP LMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIA SYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQ LQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIK MEMAV Description Functional site 1) chain B residue 50 type sequence R description binding site for residue UMP B 600 source : AC1 2) chain B residue 195 type sequence C description binding site for residue UMP B 600 source : AC1 3) chain B residue 196 type sequence H description binding site for residue UMP B 600 source : AC1 4) chain B residue 214 type sequence Q description binding site for residue UMP B 600 source : AC1 5) chain B residue 215 type sequence R description binding site for residue UMP B 600 source : AC1 6) chain B residue 216 type sequence S description binding site for residue UMP B 600 source : AC1 7) chain B residue 217 type sequence G description binding site for residue UMP B 600 source : AC1 8) chain B residue 218 type sequence D description binding site for residue UMP B 600 source : AC1 9) chain B residue 226 type sequence N description binding site for residue UMP B 600 source : AC1 10) chain B residue 256 type sequence H description binding site for residue UMP B 600 source : AC1 11) chain B residue 258 type sequence Y description binding site for residue UMP B 600 source : AC1 12) chain B residue 79 type sequence V description binding site for residue D96 B 601 source : AC2 13) chain B residue 80 type sequence F description binding site for residue D96 B 601 source : AC2 14) chain B residue 108 type sequence I description binding site for residue D96 B 601 source : AC2 15) chain B residue 112 type sequence N description binding site for residue D96 B 601 source : AC2 16) chain B residue 218 type sequence D description binding site for residue D96 B 601 source : AC2 17) chain B residue 221 type sequence L description binding site for residue D96 B 601 source : AC2 18) chain B residue 222 type sequence G description binding site for residue D96 B 601 source : AC2 19) chain B residue 224 type sequence P description binding site for residue D96 B 601 source : AC2 20) chain B residue 225 type sequence F description binding site for residue D96 B 601 source : AC2 21) chain B residue 258 type sequence Y description binding site for residue D96 B 601 source : AC2 22) chain B residue 311 type sequence M description binding site for residue D96 B 601 source : AC2 23) chain B residue 312 type sequence A description binding site for residue D96 B 601 source : AC2 24) chain A residue 50 type sequence R description binding site for residue UMP A 600 source : AC3 25) chain A residue 195 type sequence C description binding site for residue UMP A 600 source : AC3 26) chain A residue 196 type sequence H description binding site for residue UMP A 600 source : AC3 27) chain A residue 214 type sequence Q description binding site for residue UMP A 600 source : AC3 28) chain A residue 215 type sequence R description binding site for residue UMP A 600 source : AC3 29) chain A residue 216 type sequence S description binding site for residue UMP A 600 source : AC3 30) chain A residue 217 type sequence G description binding site for residue UMP A 600 source : AC3 31) chain A residue 218 type sequence D description binding site for residue UMP A 600 source : AC3 32) chain A residue 226 type sequence N description binding site for residue UMP A 600 source : AC3 33) chain A residue 256 type sequence H description binding site for residue UMP A 600 source : AC3 34) chain A residue 258 type sequence Y description binding site for residue UMP A 600 source : AC3 35) chain A residue 77 type sequence K description binding site for residue D96 A 601 source : AC4 36) chain A residue 80 type sequence F description binding site for residue D96 A 601 source : AC4 37) chain A residue 108 type sequence I description binding site for residue D96 A 601 source : AC4 38) chain A residue 109 type sequence W description binding site for residue D96 A 601 source : AC4 39) chain A residue 112 type sequence N description binding site for residue D96 A 601 source : AC4 40) chain A residue 192 type sequence L description binding site for residue D96 A 601 source : AC4 41) chain A residue 218 type sequence D description binding site for residue D96 A 601 source : AC4 42) chain A residue 221 type sequence L description binding site for residue D96 A 601 source : AC4 43) chain A residue 222 type sequence G description binding site for residue D96 A 601 source : AC4 44) chain A residue 224 type sequence P description binding site for residue D96 A 601 source : AC4 45) chain A residue 225 type sequence F description binding site for residue D96 A 601 source : AC4 46) chain A residue 258 type sequence Y description binding site for residue D96 A 601 source : AC4 47) chain A residue 312 type sequence A description binding site for residue D96 A 601 source : AC4 48) chain C residue 50 type sequence R description binding site for residue UMP C 600 source : AC5 49) chain C residue 195 type sequence C description binding site for residue UMP C 600 source : AC5 50) chain C residue 196 type sequence H description binding site for residue UMP C 600 source : AC5 51) chain C residue 214 type sequence Q description binding site for residue UMP C 600 source : AC5 52) chain C residue 215 type sequence R description binding site for residue UMP C 600 source : AC5 53) chain C residue 216 type sequence S description binding site for residue UMP C 600 source : AC5 54) chain C residue 218 type sequence D description binding site for residue UMP C 600 source : AC5 55) chain C residue 226 type sequence N description binding site for residue UMP C 600 source : AC5 56) chain C residue 256 type sequence H description binding site for residue UMP C 600 source : AC5 57) chain C residue 258 type sequence Y description binding site for residue UMP C 600 source : AC5 58) chain C residue 78 type sequence R description binding site for residue D96 C 601 source : AC6 59) chain C residue 79 type sequence V description binding site for residue D96 C 601 source : AC6 60) chain C residue 80 type sequence F description binding site for residue D96 C 601 source : AC6 61) chain C residue 108 type sequence I description binding site for residue D96 C 601 source : AC6 62) chain C residue 112 type sequence N description binding site for residue D96 C 601 source : AC6 63) chain C residue 218 type sequence D description binding site for residue D96 C 601 source : AC6 64) chain C residue 221 type sequence L description binding site for residue D96 C 601 source : AC6 65) chain C residue 222 type sequence G description binding site for residue D96 C 601 source : AC6 66) chain C residue 225 type sequence F description binding site for residue D96 C 601 source : AC6 67) chain C residue 258 type sequence Y description binding site for residue D96 C 601 source : AC6 68) chain C residue 311 type sequence M description binding site for residue D96 C 601 source : AC6 69) chain C residue 312 type sequence A description binding site for residue D96 C 601 source : AC6 70) chain D residue 50 type sequence R description binding site for residue UMP D 600 source : AC7 71) chain D residue 195 type sequence C description binding site for residue UMP D 600 source : AC7 72) chain D residue 196 type sequence H description binding site for residue UMP D 600 source : AC7 73) chain D residue 214 type sequence Q description binding site for residue UMP D 600 source : AC7 74) chain D residue 215 type sequence R description binding site for residue UMP D 600 source : AC7 75) chain D residue 216 type sequence S description binding site for residue UMP D 600 source : AC7 76) chain D residue 217 type sequence G description binding site for residue UMP D 600 source : AC7 77) chain D residue 218 type sequence D description binding site for residue UMP D 600 source : AC7 78) chain D residue 226 type sequence N description binding site for residue UMP D 600 source : AC7 79) chain D residue 256 type sequence H description binding site for residue UMP D 600 source : AC7 80) chain D residue 258 type sequence Y description binding site for residue UMP D 600 source : AC7 81) chain D residue 77 type sequence K description binding site for residue D96 D 601 source : AC8 82) chain D residue 78 type sequence R description binding site for residue D96 D 601 source : AC8 83) chain D residue 80 type sequence F description binding site for residue D96 D 601 source : AC8 84) chain D residue 108 type sequence I description binding site for residue D96 D 601 source : AC8 85) chain D residue 109 type sequence W description binding site for residue D96 D 601 source : AC8 86) chain D residue 112 type sequence N description binding site for residue D96 D 601 source : AC8 87) chain D residue 192 type sequence L description binding site for residue D96 D 601 source : AC8 88) chain D residue 218 type sequence D description binding site for residue D96 D 601 source : AC8 89) chain D residue 221 type sequence L description binding site for residue D96 D 601 source : AC8 90) chain D residue 222 type sequence G description binding site for residue D96 D 601 source : AC8 91) chain D residue 258 type sequence Y description binding site for residue D96 D 601 source : AC8 92) chain D residue 311 type sequence M description binding site for residue D96 D 601 source : AC8 93) chain D residue 312 type sequence A description binding site for residue D96 D 601 source : AC8 94) chain B residue 195 type ACT_SITE sequence C description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 95) chain A residue 195 type ACT_SITE sequence C description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 96) chain C residue 218 type ACT_SITE sequence D description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 97) chain D residue 195 type ACT_SITE sequence C description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 98) chain B residue 50 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 99) chain B residue 226 type BINDING sequence N description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 100) chain A residue 50 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 101) chain A residue 226 type BINDING sequence N description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 102) chain C residue 73 type BINDING sequence L description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 103) chain C residue 249 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 104) chain D residue 50 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 105) chain D residue 226 type BINDING sequence N description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 106) chain B residue 175 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 107) chain A residue 175 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 108) chain C residue 198 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 109) chain D residue 175 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 110) chain B residue 195 type BINDING sequence C description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 111) chain D residue 195 type BINDING sequence C description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 112) chain D residue 215 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 113) chain D residue 256 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 114) chain B residue 215 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 115) chain B residue 256 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 116) chain A residue 195 type BINDING sequence C description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 117) chain A residue 215 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 118) chain A residue 256 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 119) chain C residue 218 type BINDING sequence D description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 120) chain C residue 238 type BINDING sequence A description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 121) chain C residue 279 type BINDING sequence L description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 122) chain B residue 218 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 123) chain B residue 312 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 124) chain A residue 218 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 125) chain A residue 312 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 126) chain C residue 241 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 127) chain D residue 218 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 128) chain D residue 312 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 129) chain B residue 114 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 130) chain A residue 114 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 131) chain C residue 137 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 132) chain D residue 114 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 133) chain B residue 175-203 type prosite sequence RRIIMCAWNPRDLPLMALPPCHALCQFYV description THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriImcaWNprdlplma.....LpPCHalcQFyV source prosite : PS00091 134) chain B residue 287 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 135) chain D residue 287 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 136) chain D residue 292 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 137) chain D residue 308 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 138) chain B residue 292 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 139) chain B residue 308 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 140) chain A residue 287 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 141) chain A residue 292 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 142) chain A residue 308 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 143) chain C residue 310 type CROSSLNK sequence E 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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