7S81
Structure of human PARP1 domains (Zn1, Zn3, WGR, HD) bound to a DNA double strand break.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0008270 | molecular_function | zinc ion binding |
| B | 0008270 | molecular_function | zinc ion binding |
| C | 0003950 | molecular_function | NAD+-protein poly-ADP-ribosyltransferase activity |
| F | 0003677 | molecular_function | DNA binding |
| F | 0008270 | molecular_function | zinc ion binding |
| G | 0008270 | molecular_function | zinc ion binding |
| H | 0003950 | molecular_function | NAD+-protein poly-ADP-ribosyltransferase activity |
| I | 0003677 | molecular_function | DNA binding |
| I | 0008270 | molecular_function | zinc ion binding |
| J | 0008270 | molecular_function | zinc ion binding |
| K | 0003950 | molecular_function | NAD+-protein poly-ADP-ribosyltransferase activity |
| N | 0003677 | molecular_function | DNA binding |
| N | 0008270 | molecular_function | zinc ion binding |
| O | 0008270 | molecular_function | zinc ion binding |
| P | 0003950 | molecular_function | NAD+-protein poly-ADP-ribosyltransferase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00347 |
| Number of Residues | 36 |
| Details | ZF_PARP_1 Zinc finger poly(ADP-ribose) polymerase (PARP)-type signature. CKkCsesIpKdslRmaimvqspmfdgkvph..WYHfsC |
| Chain | Residue | Details |
| N | CYS21-CYS56 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01351, ECO:0000269|PubMed:18055453, ECO:0000269|PubMed:22582261, ECO:0007744|PDB:2RIQ, ECO:0007744|PDB:4DQY, ECO:0007744|PDB:4OPX, ECO:0007744|PDB:4OQA, ECO:0007744|PDB:4OQB |
| Chain | Residue | Details |
| G | CYS295 | |
| J | CYS298 | |
| J | CYS311 | |
| J | CYS321 | |
| B | CYS295 | |
| B | CYS298 | |
| B | CYS311 | |
| B | CYS321 | |
| G | CYS298 | |
| G | CYS311 | |
| G | CYS321 | |
| O | CYS295 | |
| O | CYS298 | |
| O | CYS311 | |
| O | CYS321 | |
| J | CYS295 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| G | SER274 | |
| A | CYS24 | |
| A | HIS53 | |
| A | CYS56 | |
| F | CYS21 | |
| F | CYS24 | |
| F | HIS53 | |
| F | CYS56 | |
| G | SER277 | |
| O | SER274 | |
| O | SER277 | |
| J | SER274 | |
| J | SER277 | |
| B | SER274 | |
| B | SER277 | |
| A | CYS21 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| G | SER364 | |
| O | SER364 | |
| J | SER364 | |
| B | SER364 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| G | LYS249 | |
| I | SER41 | |
| O | LYS249 | |
| F | SER41 | |
| J | LYS249 | |
| B | LYS249 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| C | LYS528 | |
| K | LYS528 | |
| P | LYS528 | |
| H | LYS528 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| C | ALA762 | |
| K | ALA762 | |
| P | ALA762 | |
| H | ALA762 |
