5A00
Structure of human PARP1 catalytic domain bound to an isoindolinone inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003950 | molecular_function | NAD+ ADP-ribosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE D7N A 2012 |
| Chain | Residue |
| A | GLN759 |
| A | ALA898 |
| A | LYS903 |
| A | SER904 |
| A | TYR907 |
| A | GLU988 |
| A | VAL762 |
| A | HIS862 |
| A | GLY863 |
| A | THR887 |
| A | GLY888 |
| A | TYR889 |
| A | TYR896 |
| A | PHE897 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2013 |
| Chain | Residue |
| A | LYS903 |
| A | LEU985 |
| A | TYR986 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2014 |
| Chain | Residue |
| A | ARG858 |
| A | ASN928 |
| A | MET929 |
| A | LYS945 |
| A | LYS949 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: For poly [ADP-ribose] polymerase activity => ECO:0000305|PubMed:32028527, ECO:0000305|PubMed:7852410, ECO:0000305|PubMed:9315851 |
| Chain | Residue | Details |
| A | GLU988 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9UGN5 |
| Chain | Residue | Details |
| A | HIS862 | |
| A | GLY871 | |
| A | ARG878 | |
| A | SER904 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER782 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER786 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| 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 |
| A | LYS748 |
