eF-site ID 6ojv-C PDB Code 6ojv Chain C 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 C:  SELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLR DEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKI WDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRD MESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLP LMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIA SYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQ LQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIK MEMAV Description Functional site 1) chain C residue 50 type sequence R description binding site for residue UMP C 600 source : AC5 2) chain C residue 192 type sequence L description binding site for residue UMP C 600 source : AC5 3) chain C residue 195 type sequence C description binding site for residue UMP C 600 source : AC5 4) chain C residue 196 type sequence H description binding site for residue UMP C 600 source : AC5 5) chain C residue 214 type sequence Q description binding site for residue UMP C 600 source : AC5 6) chain C residue 215 type sequence R description binding site for residue UMP C 600 source : AC5 7) chain C residue 216 type sequence S description binding site for residue UMP C 600 source : AC5 8) chain C residue 217 type sequence G description binding site for residue UMP C 600 source : AC5 9) chain C residue 218 type sequence D description binding site for residue UMP C 600 source : AC5 10) chain C residue 226 type sequence N description binding site for residue UMP C 600 source : AC5 11) chain C residue 256 type sequence H description binding site for residue UMP C 600 source : AC5 12) chain C residue 258 type sequence Y description binding site for residue UMP C 600 source : AC5 13) chain C residue 108 type sequence I description binding site for residue 2XB C 601 source : AC6 14) chain C residue 112 type sequence N description binding site for residue 2XB C 601 source : AC6 15) chain C residue 218 type sequence D description binding site for residue 2XB C 601 source : AC6 16) chain C residue 221 type sequence L description binding site for residue 2XB C 601 source : AC6 17) chain C residue 222 type sequence G description binding site for residue 2XB C 601 source : AC6 18) chain C residue 258 type sequence Y description binding site for residue 2XB C 601 source : AC6 19) chain C residue 311 type sequence M description binding site for residue 2XB C 601 source : AC6 20) chain C residue 312 type sequence A description binding site for residue 2XB C 601 source : AC6 21) chain C residue 218 type ACT_SITE sequence D description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 22) chain C residue 73 type BINDING sequence L description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 23) chain C residue 249 type BINDING sequence I description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 24) chain C residue 198 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI3 25) chain C residue 218 type BINDING sequence D description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 26) chain C residue 238 type BINDING sequence A description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 27) chain C residue 279 type BINDING sequence L description in other chain => ECO:0000250|UniProtKB:P45352 source Swiss-Prot : SWS_FT_FI4 28) chain C residue 241 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI5 29) 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 30) 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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