eF-site ID 4opx-ACDFMN PDB Code 4opx Chain A, C, D, F, M, N click to enlarge Title Structure of Human PARP-1 bound to a DNA double strand break in complex with (2R)-5-fluoro-2-methyl-2,3-dihydro-1-benzofuran-7-carboxamide Classification TRANSFERASE/DNA/TRANSFERASE INHIBITOR Compound Poly [ADP-ribose] polymerase 1 Source Homo sapiens (Human) (4OPX) Sequence A:  DKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFD GKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKV KKTAEASKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCS TNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEE CSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPK EFREISYLKKLKVKKQDRIFPP C:  AAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYY KLQLLWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLY EEKTGNAWHSKNFTKYPKKFYPLEIDKSKLPKPVQDLIKM IFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSE VQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNA DSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYE KLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVID IFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQ GLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDP IGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTT PDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIA QVNLKYLLKLKFNFKT D:  DKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFD GKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKV KKTAEASKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCS TNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEE CSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPK EFREISYLKKLKVKKQDRIFPP F:  AAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYY KLQLLWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLY EEKTGNAWHSKNFTKYPKKFYPLEIDKSKLPKPVQDLIKM IFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSE VQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNA DSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYE KLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVID IFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQ GLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDP IGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTT PDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIA QVNLKYLLKLKFNFKT M:  GCCTACCGGTTCGCGAACCGGTAGGC N:  GCCTACCGGTTCGCGAACCGGTAGGC Description Functional site 1) chain A residue 21 type sequence C description BINDING SITE FOR RESIDUE ZN A 401 source : AC1 2) chain A residue 24 type sequence C description BINDING SITE FOR RESIDUE ZN A 401 source : AC1 3) chain A residue 53 type sequence H description BINDING SITE FOR RESIDUE ZN A 401 source : AC1 4) chain A residue 56 type sequence C description BINDING SITE FOR RESIDUE ZN A 401 source : AC1 5) chain A residue 295 type sequence C description BINDING SITE FOR RESIDUE ZN A 402 source : AC2 6) chain A residue 298 type sequence C description BINDING SITE FOR RESIDUE ZN A 402 source : AC2 7) chain A residue 311 type sequence C description BINDING SITE FOR RESIDUE ZN A 402 source : AC2 8) chain A residue 321 type sequence C description BINDING SITE FOR RESIDUE ZN A 402 source : AC2 9) chain C residue 862 type sequence H description BINDING SITE FOR RESIDUE 2UR C 1101 source : AC3 10) chain C residue 863 type sequence G description BINDING SITE FOR RESIDUE 2UR C 1101 source : AC3 11) chain C residue 896 type sequence Y description BINDING SITE FOR RESIDUE 2UR C 1101 source : AC3 12) chain C residue 897 type sequence F description BINDING SITE FOR RESIDUE 2UR C 1101 source : AC3 13) chain C residue 898 type sequence A description BINDING SITE FOR RESIDUE 2UR C 1101 source : AC3 14) chain C residue 903 type sequence K description BINDING SITE FOR RESIDUE 2UR C 1101 source : AC3 15) chain C residue 904 type sequence S description BINDING SITE FOR RESIDUE 2UR C 1101 source : AC3 16) chain C residue 907 type sequence Y description BINDING SITE FOR RESIDUE 2UR C 1101 source : AC3 17) chain D residue 21 type sequence C description BINDING SITE FOR RESIDUE ZN D 401 source : AC4 18) chain D residue 24 type sequence C description BINDING SITE FOR RESIDUE ZN D 401 source : AC4 19) chain D residue 53 type sequence H description BINDING SITE FOR RESIDUE ZN D 401 source : AC4 20) chain D residue 56 type sequence C description BINDING SITE FOR RESIDUE ZN D 401 source : AC4 21) chain D residue 295 type sequence C description BINDING SITE FOR RESIDUE ZN D 402 source : AC5 22) chain D residue 298 type sequence C description BINDING SITE FOR RESIDUE ZN D 402 source : AC5 23) chain D residue 311 type sequence C description BINDING SITE FOR RESIDUE ZN D 402 source : AC5 24) chain D residue 321 type sequence C description BINDING SITE FOR RESIDUE ZN D 402 source : AC5 25) chain A residue 21-56 type prosite sequence CKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSC description ZF_PARP_1 Zinc finger poly(ADP-ribose) polymerase (PARP)-type signature. CKkCsesIpKdslRmaimvqspmfdgkvph..WYHfsC source prosite : PS00347 26) chain C residue 988 type ACT_SITE sequence E description For poly [ADP-ribose] polymerase activity => ECO:0000305|PubMed:32028527, ECO:0000305|PubMed:7852410, ECO:0000305|PubMed:9315851 source Swiss-Prot : SWS_FT_FI1 27) chain F residue 988 type ACT_SITE sequence E description For poly [ADP-ribose] polymerase activity => ECO:0000305|PubMed:32028527, ECO:0000305|PubMed:7852410, ECO:0000305|PubMed:9315851 source Swiss-Prot : SWS_FT_FI1 28) chain D residue 249 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_FI10 29) chain C residue 748 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI11 30) chain F residue 748 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI11 31) chain C residue 862 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q9UGN5 source Swiss-Prot : SWS_FT_FI2 32) chain C residue 871 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q9UGN5 source Swiss-Prot : SWS_FT_FI2 33) chain C residue 878 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:Q9UGN5 source Swiss-Prot : SWS_FT_FI2 34) chain C residue 904 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q9UGN5 source Swiss-Prot : SWS_FT_FI2 35) chain F residue 862 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q9UGN5 source Swiss-Prot : SWS_FT_FI2 36) chain F residue 871 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q9UGN5 source Swiss-Prot : SWS_FT_FI2 37) chain F residue 878 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:Q9UGN5 source Swiss-Prot : SWS_FT_FI2 38) chain F residue 904 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q9UGN5 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 311 type MOD_RES sequence C description ADP-ribosylserine => ECO:0000269|PubMed:28190768, ECO:0000269|PubMed:29954836, ECO:0000269|PubMed:34210965, ECO:0000269|PubMed:34625544 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 321 type MOD_RES sequence C description ADP-ribosylserine => ECO:0000269|PubMed:28190768, ECO:0000269|PubMed:29954836, ECO:0000269|PubMed:34210965, ECO:0000269|PubMed:34625544 source Swiss-Prot : SWS_FT_FI3 41) chain D residue 295 type MOD_RES sequence C description ADP-ribosylserine => ECO:0000269|PubMed:28190768, ECO:0000269|PubMed:29954836, ECO:0000269|PubMed:34210965, ECO:0000269|PubMed:34625544 source Swiss-Prot : SWS_FT_FI3 42) chain D residue 298 type MOD_RES sequence C description ADP-ribosylserine => ECO:0000269|PubMed:28190768, ECO:0000269|PubMed:29954836, ECO:0000269|PubMed:34210965, ECO:0000269|PubMed:34625544 source Swiss-Prot : SWS_FT_FI3 43) chain D residue 311 type MOD_RES sequence C description ADP-ribosylserine => ECO:0000269|PubMed:28190768, ECO:0000269|PubMed:29954836, ECO:0000269|PubMed:34210965, ECO:0000269|PubMed:34625544 source Swiss-Prot : SWS_FT_FI3 44) chain D residue 321 type MOD_RES sequence C description ADP-ribosylserine => ECO:0000269|PubMed:28190768, ECO:0000269|PubMed:29954836, ECO:0000269|PubMed:34210965, ECO:0000269|PubMed:34625544 source Swiss-Prot : SWS_FT_FI3 45) chain C residue 594 type MOD_RES sequence T description Phosphothreonine; by PRKDC => ECO:0000269|PubMed:35460603 source Swiss-Prot : SWS_FT_FI6 46) chain F residue 594 type MOD_RES sequence T description Phosphothreonine; by PRKDC => ECO:0000269|PubMed:35460603 source Swiss-Prot : SWS_FT_FI6 47) chain C residue 600 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 48) chain C residue 621 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 49) chain F residue 600 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 50) chain F residue 621 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 51) chain C residue 782 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 52) chain F residue 782 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 53) chain D residue 274 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 54) chain D residue 277 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 55) chain C residue 786 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9 56) chain F residue 786 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9

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