eF-site ID 6ojv-B PDB Code 6ojv Chain B 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 B:  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 B residue 195 type ACT_SITE sequence C description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 23) chain B residue 50 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 24) chain B residue 226 type BINDING sequence N description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 25) chain B residue 175-203 type prosite sequence RRIIMCAWNPRDLPLMALPPCHALCQFYV description THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriImcaWNprdlplma.....LpPCHalcQFyV source prosite : PS00091 26) chain B residue 175 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 27) chain B residue 195 type BINDING sequence C description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 28) chain B residue 215 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 29) chain B residue 256 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 30) chain B residue 218 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 31) chain B residue 312 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 32) 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 33) 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 34) 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 35) 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

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