eF-site ID 4pjt-C PDB Code 4pjt Chain C click to enlarge Title Structure of PARP1 catalytic domain bound to inhibitor BMN 673 Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Poly [ADP-ribose] polymerase 1 Source Homo sapiens (Human) (PARP1_HUMAN) Sequence C:  KSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKL SKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIP HDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGG SSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHAT THNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGS RTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKS ANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKG KHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSL LYNEYIVYDIAQVNLKYLLKLKFNFK Description Functional site 1) chain C residue 937 type sequence H description binding site for residue SO4 A 1104 source : AC4 2) chain C residue 946 type sequence H description binding site for residue SO4 B 1104 source : AD2 3) chain C residue 903 type sequence K description binding site for residue SO4 C 1101 source : AD5 4) chain C residue 985 type sequence L description binding site for residue SO4 C 1101 source : AD5 5) chain C residue 986 type sequence Y description binding site for residue SO4 C 1101 source : AD5 6) chain C residue 838 type sequence K description binding site for residue SO4 C 1102 source : AD6 7) chain C residue 1000 type sequence K description binding site for residue SO4 C 1102 source : AD6 8) chain C residue 702 type sequence S description binding site for residue SO4 C 1103 source : AD7 9) chain C residue 703 type sequence K description binding site for residue SO4 C 1103 source : AD7 10) chain C residue 704 type sequence R description binding site for residue SO4 C 1103 source : AD7 11) chain C residue 759 type sequence Q description binding site for residue 2YQ C 1104 source : AD8 12) chain C residue 862 type sequence H description binding site for residue 2YQ C 1104 source : AD8 13) chain C residue 863 type sequence G description binding site for residue 2YQ C 1104 source : AD8 14) chain C residue 888 type sequence G description binding site for residue 2YQ C 1104 source : AD8 15) chain C residue 889 type sequence Y description binding site for residue 2YQ C 1104 source : AD8 16) chain C residue 896 type sequence Y description binding site for residue 2YQ C 1104 source : AD8 17) chain C residue 897 type sequence F description binding site for residue 2YQ C 1104 source : AD8 18) chain C residue 898 type sequence A description binding site for residue 2YQ C 1104 source : AD8 19) chain C residue 903 type sequence K description binding site for residue 2YQ C 1104 source : AD8 20) chain C residue 904 type sequence S description binding site for residue 2YQ C 1104 source : AD8 21) chain C residue 907 type sequence Y description binding site for residue 2YQ C 1104 source : AD8 22) chain C residue 988 type sequence E description binding site for residue 2YQ C 1104 source : AD8 23) chain C residue 888 type sequence G description binding site for residue GOL C 1105 source : AD9 24) chain C residue 889 type sequence Y description binding site for residue GOL C 1105 source : AD9 25) chain C residue 890 type sequence M description binding site for residue GOL C 1105 source : AD9 26) chain C residue 896 type sequence Y description binding site for residue GOL C 1105 source : AD9 27) chain C residue 988 type sequence E description binding site for residue GOL C 1105 source : AD9 28) chain C residue 843 type sequence G description binding site for residue SO4 D 1101 source : AE1 29) chain C residue 845 type sequence C description binding site for residue SO4 D 1101 source : AE1 30) chain C residue 846 type sequence Q description binding site for residue SO4 D 1101 source : AE1 31) 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 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 C residue 862 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q9UGN5 source Swiss-Prot : SWS_FT_FI2 36) chain C residue 786 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 37) 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_FI5

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