eF-site ID 4opx-C PDB Code 4opx Chain C 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 C:  AAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYY KLQLLWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLY EEKTGNAWHSKNFTKYPKKFYPLEIDKSKLPKPVQDLIKM IFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSE VQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNA DSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYE KLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVID IFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQ GLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDP IGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTT PDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIA QVNLKYLLKLKFNFKT Description Functional site 1) chain C residue 862 type sequence H description BINDING SITE FOR RESIDUE 2UR C 1101 source : AC3 2) chain C residue 863 type sequence G description BINDING SITE FOR RESIDUE 2UR C 1101 source : AC3 3) chain C residue 896 type sequence Y description BINDING SITE FOR RESIDUE 2UR C 1101 source : AC3 4) chain C residue 897 type sequence F description BINDING SITE FOR RESIDUE 2UR C 1101 source : AC3 5) chain C residue 898 type sequence A description BINDING SITE FOR RESIDUE 2UR C 1101 source : AC3 6) chain C residue 903 type sequence K description BINDING SITE FOR RESIDUE 2UR C 1101 source : AC3 7) chain C residue 904 type sequence S description BINDING SITE FOR RESIDUE 2UR C 1101 source : AC3 8) chain C residue 907 type sequence Y description BINDING SITE FOR RESIDUE 2UR C 1101 source : AC3 9) 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 10) 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 11) chain C residue 862 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q9UGN5 source Swiss-Prot : SWS_FT_FI2 12) chain C residue 871 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q9UGN5 source Swiss-Prot : SWS_FT_FI2 13) chain C residue 878 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:Q9UGN5 source Swiss-Prot : SWS_FT_FI2 14) chain C residue 904 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q9UGN5 source Swiss-Prot : SWS_FT_FI2 15) 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 16) chain C residue 786 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9 17) chain C residue 594 type MOD_RES sequence T description Phosphothreonine; by PRKDC => ECO:0000269|PubMed:35460603 source Swiss-Prot : SWS_FT_FI6 18) chain C residue 600 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 19) chain C residue 621 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7

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