eF-site ID 6ojv-ABCD PDB Code 6ojv 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-L-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 108 type sequence I description binding site for residue 2XB B 601 source : AC2 13) chain B residue 112 type sequence N description binding site for residue 2XB B 601 source : AC2 14) chain B residue 192 type sequence L description binding site for residue 2XB B 601 source : AC2 15) chain B residue 218 type sequence D description binding site for residue 2XB B 601 source : AC2 16) chain B residue 221 type sequence L description binding site for residue 2XB B 601 source : AC2 17) chain B residue 222 type sequence G description binding site for residue 2XB B 601 source : AC2 18) chain B residue 225 type sequence F description binding site for residue 2XB B 601 source : AC2 19) chain B residue 258 type sequence Y description binding site for residue 2XB B 601 source : AC2 20) chain B residue 311 type sequence M description binding site for residue 2XB B 601 source : AC2 21) chain B residue 312 type sequence A description binding site for residue 2XB B 601 source : AC2 22) chain A residue 50 type sequence R description binding site for residue UMP A 600 source : AC3 23) chain A residue 195 type sequence C description binding site for residue UMP A 600 source : AC3 24) chain A residue 196 type sequence H description binding site for residue UMP A 600 source : AC3 25) chain A residue 214 type sequence Q description binding site for residue UMP A 600 source : AC3 26) chain A residue 215 type sequence R description binding site for residue UMP A 600 source : AC3 27) chain A residue 216 type sequence S description binding site for residue UMP A 600 source : AC3 28) chain A residue 217 type sequence G description binding site for residue UMP A 600 source : AC3 29) chain A residue 218 type sequence D description binding site for residue UMP A 600 source : AC3 30) chain A residue 226 type sequence N description binding site for residue UMP A 600 source : AC3 31) chain A residue 256 type sequence H description binding site for residue UMP A 600 source : AC3 32) chain A residue 258 type sequence Y description binding site for residue UMP A 600 source : AC3 33) chain D residue 175 type sequence R description binding site for residue UMP A 600 source : AC3 34) chain D residue 176 type sequence R description binding site for residue UMP A 600 source : AC3 35) chain A residue 108 type sequence I description binding site for residue 2XB A 601 source : AC4 36) chain A residue 109 type sequence W description binding site for residue 2XB A 601 source : AC4 37) chain A residue 112 type sequence N description binding site for residue 2XB A 601 source : AC4 38) chain A residue 192 type sequence L description binding site for residue 2XB A 601 source : AC4 39) chain A residue 218 type sequence D description binding site for residue 2XB A 601 source : AC4 40) chain A residue 222 type sequence G description binding site for residue 2XB A 601 source : AC4 41) chain A residue 258 type sequence Y description binding site for residue 2XB A 601 source : AC4 42) chain A residue 311 type sequence M description binding site for residue 2XB A 601 source : AC4 43) chain A residue 312 type sequence A description binding site for residue 2XB A 601 source : AC4 44) chain C residue 50 type sequence R description binding site for residue UMP C 600 source : AC5 45) chain C residue 192 type sequence L description binding site for residue UMP C 600 source : AC5 46) chain C residue 195 type sequence C description binding site for residue UMP C 600 source : AC5 47) chain C residue 196 type sequence H description binding site for residue UMP C 600 source : AC5 48) chain C residue 214 type sequence Q description binding site for residue UMP C 600 source : AC5 49) chain C residue 215 type sequence R description binding site for residue UMP C 600 source : AC5 50) chain C residue 216 type sequence S description binding site for residue UMP C 600 source : AC5 51) chain C residue 217 type sequence G description binding site for residue UMP C 600 source : AC5 52) chain C residue 218 type sequence D description binding site for residue UMP C 600 source : AC5 53) chain C residue 226 type sequence N description binding site for residue UMP C 600 source : AC5 54) chain C residue 256 type sequence H description binding site for residue UMP C 600 source : AC5 55) chain C residue 258 type sequence Y description binding site for residue UMP C 600 source : AC5 56) chain C residue 108 type sequence I description binding site for residue 2XB C 601 source : AC6 57) chain C residue 112 type sequence N description binding site for residue 2XB C 601 source : AC6 58) chain C residue 218 type sequence D description binding site for residue 2XB C 601 source : AC6 59) chain C residue 221 type sequence L description binding site for residue 2XB C 601 source : AC6 60) chain C residue 222 type sequence G description binding site for residue 2XB C 601 source : AC6 61) chain C residue 258 type sequence Y description binding site for residue 2XB C 601 source : AC6 62) chain C residue 311 type sequence M description binding site for residue 2XB C 601 source : AC6 63) chain C residue 312 type sequence A description binding site for residue 2XB C 601 source : AC6 64) chain A residue 175 type sequence R description binding site for residue UMP D 600 source : AC7 65) chain A residue 176 type sequence R description binding site for residue UMP D 600 source : AC7 66) chain D residue 50 type sequence R description binding site for residue UMP D 600 source : AC7 67) chain D residue 195 type sequence C description binding site for residue UMP D 600 source : AC7 68) chain D residue 196 type sequence H description binding site for residue UMP D 600 source : AC7 69) chain D residue 214 type sequence Q description binding site for residue UMP D 600 source : AC7 70) chain D residue 215 type sequence R description binding site for residue UMP D 600 source : AC7 71) chain D residue 216 type sequence S description binding site for residue UMP D 600 source : AC7 72) chain D residue 218 type sequence D description binding site for residue UMP D 600 source : AC7 73) chain D residue 226 type sequence N description binding site for residue UMP D 600 source : AC7 74) chain D residue 256 type sequence H description binding site for residue UMP D 600 source : AC7 75) chain D residue 258 type sequence Y description binding site for residue UMP D 600 source : AC7 76) chain D residue 77 type sequence K description binding site for residue 2XB D 601 source : AC8 77) chain D residue 80 type sequence F description binding site for residue 2XB D 601 source : AC8 78) chain D residue 108 type sequence I description binding site for residue 2XB D 601 source : AC8 79) chain D residue 112 type sequence N description binding site for residue 2XB D 601 source : AC8 80) chain D residue 218 type sequence D description binding site for residue 2XB D 601 source : AC8 81) chain D residue 222 type sequence G description binding site for residue 2XB D 601 source : AC8 82) chain D residue 225 type sequence F description binding site for residue 2XB D 601 source : AC8 83) chain D residue 311 type sequence M description binding site for residue 2XB D 601 source : AC8 84) chain D residue 312 type sequence A description binding site for residue 2XB D 601 source : AC8 85) chain B residue 175-203 type prosite sequence RRIIMCAWNPRDLPLMALPPCHALCQFYV description THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriImcaWNprdlplma.....LpPCHalcQFyV source prosite : PS00091 86) 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 87) 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 88) 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 89) 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 90) 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 91) 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 92) 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 93) 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 94) 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 95) 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 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 195 type ACT_SITE sequence C description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 99) chain A residue 195 type ACT_SITE sequence C description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 100) chain C residue 198 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 101) chain D residue 175 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 102) chain B residue 175 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 103) chain A residue 175 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 104) chain D residue 195 type BINDING sequence C description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 105) chain D residue 215 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 106) chain D residue 256 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 107) chain A residue 215 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 108) chain A residue 256 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 109) chain C residue 218 type BINDING sequence D description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 110) chain C residue 238 type BINDING sequence A description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 111) chain C residue 279 type BINDING sequence L description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 112) chain B residue 256 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 113) chain A residue 195 type BINDING sequence C description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 114) chain B residue 195 type BINDING sequence C description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 115) chain B residue 215 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 116) chain C residue 241 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 117) chain D residue 218 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 118) chain D residue 312 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 119) chain A residue 218 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 120) chain A residue 312 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 121) chain B residue 218 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 122) chain B residue 312 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 123) 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 124) 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 125) 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 126) 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 127) chain A residue 50 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 128) chain A residue 226 type BINDING sequence N description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 129) chain C residue 73 type BINDING sequence L description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 130) chain C residue 249 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 131) chain D residue 50 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 132) chain D residue 226 type BINDING sequence N description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 133) chain B residue 50 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 134) chain B residue 226 type BINDING sequence N description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2

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