eF-site ID 6oju-A PDB Code 6oju Chain A 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 Description Functional site 1) chain A residue 50 type sequence R description binding site for residue UMP A 600 source : AC3 2) chain A residue 195 type sequence C description binding site for residue UMP A 600 source : AC3 3) chain A residue 196 type sequence H description binding site for residue UMP A 600 source : AC3 4) chain A residue 214 type sequence Q description binding site for residue UMP A 600 source : AC3 5) chain A residue 215 type sequence R description binding site for residue UMP A 600 source : AC3 6) chain A residue 216 type sequence S description binding site for residue UMP A 600 source : AC3 7) chain A residue 217 type sequence G description binding site for residue UMP A 600 source : AC3 8) chain A residue 218 type sequence D description binding site for residue UMP A 600 source : AC3 9) chain A residue 226 type sequence N description binding site for residue UMP A 600 source : AC3 10) chain A residue 256 type sequence H description binding site for residue UMP A 600 source : AC3 11) chain A residue 258 type sequence Y description binding site for residue UMP A 600 source : AC3 12) chain A residue 77 type sequence K description binding site for residue D96 A 601 source : AC4 13) chain A residue 80 type sequence F description binding site for residue D96 A 601 source : AC4 14) chain A residue 108 type sequence I description binding site for residue D96 A 601 source : AC4 15) chain A residue 109 type sequence W description binding site for residue D96 A 601 source : AC4 16) chain A residue 112 type sequence N description binding site for residue D96 A 601 source : AC4 17) chain A residue 192 type sequence L description binding site for residue D96 A 601 source : AC4 18) chain A residue 218 type sequence D description binding site for residue D96 A 601 source : AC4 19) chain A residue 221 type sequence L description binding site for residue D96 A 601 source : AC4 20) chain A residue 222 type sequence G description binding site for residue D96 A 601 source : AC4 21) chain A residue 224 type sequence P description binding site for residue D96 A 601 source : AC4 22) chain A residue 225 type sequence F description binding site for residue D96 A 601 source : AC4 23) chain A residue 258 type sequence Y description binding site for residue D96 A 601 source : AC4 24) chain A residue 312 type sequence A description binding site for residue D96 A 601 source : AC4 25) 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 26) 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 27) 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 28) chain A residue 195 type ACT_SITE sequence C description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 50 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 226 type BINDING sequence N description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 175 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 215 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 33) chain A residue 256 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 195 type BINDING sequence C description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 218 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 36) chain A residue 312 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 37) 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

Display surface Download Links