eF-site ID 6oju-D PDB Code 6oju Chain 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 D:  SELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLR DEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKI WDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRD MESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLP LMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIA SYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQ LQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIK MEMAV Description Functional site 1) chain D residue 50 type sequence R description binding site for residue UMP D 600 source : AC7 2) chain D residue 195 type sequence C description binding site for residue UMP D 600 source : AC7 3) chain D residue 196 type sequence H description binding site for residue UMP D 600 source : AC7 4) chain D residue 214 type sequence Q description binding site for residue UMP D 600 source : AC7 5) chain D residue 215 type sequence R description binding site for residue UMP D 600 source : AC7 6) chain D residue 216 type sequence S description binding site for residue UMP D 600 source : AC7 7) chain D residue 217 type sequence G description binding site for residue UMP D 600 source : AC7 8) chain D residue 218 type sequence D description binding site for residue UMP D 600 source : AC7 9) chain D residue 226 type sequence N description binding site for residue UMP D 600 source : AC7 10) chain D residue 256 type sequence H description binding site for residue UMP D 600 source : AC7 11) chain D residue 258 type sequence Y description binding site for residue UMP D 600 source : AC7 12) chain D residue 77 type sequence K description binding site for residue D96 D 601 source : AC8 13) chain D residue 78 type sequence R description binding site for residue D96 D 601 source : AC8 14) chain D residue 80 type sequence F description binding site for residue D96 D 601 source : AC8 15) chain D residue 108 type sequence I description binding site for residue D96 D 601 source : AC8 16) chain D residue 109 type sequence W description binding site for residue D96 D 601 source : AC8 17) chain D residue 112 type sequence N description binding site for residue D96 D 601 source : AC8 18) chain D residue 192 type sequence L description binding site for residue D96 D 601 source : AC8 19) chain D residue 218 type sequence D description binding site for residue D96 D 601 source : AC8 20) chain D residue 221 type sequence L description binding site for residue D96 D 601 source : AC8 21) chain D residue 222 type sequence G description binding site for residue D96 D 601 source : AC8 22) chain D residue 258 type sequence Y description binding site for residue D96 D 601 source : AC8 23) chain D residue 311 type sequence M description binding site for residue D96 D 601 source : AC8 24) chain D residue 312 type sequence A description binding site for residue D96 D 601 source : AC8 25) 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 26) 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 27) 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 28) chain D residue 195 type ACT_SITE sequence C description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 29) chain D residue 50 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 30) chain D residue 226 type BINDING sequence N description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 31) chain D residue 175 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 32) chain D residue 195 type BINDING sequence C description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 33) chain D residue 215 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 34) chain D residue 256 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 35) chain D residue 218 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 36) chain D residue 312 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 37) 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

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