4HHY
Crystal structure of PARP catalytic domain in complex with novel inhibitors
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 15R A 401 |
| Chain | Residue |
| A | LEU108 |
| A | TYR235 |
| A | SER243 |
| A | TYR246 |
| A | GLU327 |
| A | PEG403 |
| A | HOH508 |
| A | HOH520 |
| A | ASP109 |
| A | HIS201 |
| A | GLY202 |
| A | ARG217 |
| A | ILE218 |
| A | ALA219 |
| A | TYR228 |
| A | GLY233 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | LYS242 |
| A | LEU323 |
| A | LEU324 |
| A | TYR325 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEG A 403 |
| Chain | Residue |
| A | ASP109 |
| A | GLY210 |
| A | ILE211 |
| A | GLN214 |
| A | GLY215 |
| A | ARG217 |
| A | 15R401 |
| A | HOH531 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 15R B 401 |
| Chain | Residue |
| B | TYR49 |
| B | ASP109 |
| B | HIS201 |
| B | GLY202 |
| B | ARG217 |
| B | ILE218 |
| B | ALA219 |
| B | TYR228 |
| B | GLY233 |
| B | TYR235 |
| B | SER243 |
| B | TYR246 |
| B | HOH510 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 402 |
| Chain | Residue |
| B | LYS242 |
| B | LEU323 |
| B | LEU324 |
| B | TYR325 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 15R C 401 |
| Chain | Residue |
| C | LEU108 |
| C | ASP109 |
| C | VAL112 |
| C | HIS201 |
| C | GLY202 |
| C | ARG217 |
| C | ILE218 |
| C | ALA219 |
| C | GLY233 |
| C | TYR235 |
| C | PHE236 |
| C | SER243 |
| C | TYR246 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 15R D 401 |
| Chain | Residue |
| D | LEU108 |
| D | ASP109 |
| D | VAL112 |
| D | HIS201 |
| D | GLY202 |
| D | ARG217 |
| D | ILE218 |
| D | ALA219 |
| D | PRO220 |
| D | TYR228 |
| D | GLY233 |
| D | TYR235 |
| D | PHE236 |
| D | SER243 |
| D | TYR246 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 117 |
| Details | Domain: {"description":"PARP alpha-helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00398","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"For poly [ADP-ribose] polymerase activity","evidences":[{"source":"PubMed","id":"32028527","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"7852410","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9315851","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9UGN5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
