4B1G
Structure of unliganded human PARG catalytic domain
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DTV A 1603 |
| Chain | Residue |
| A | LYS599 |
| A | LEU602 |
| A | CYS603 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1963 |
| Chain | Residue |
| A | VAL562 |
| A | HOH2095 |
| A | TYR521 |
| A | PRO522 |
| A | ARG535 |
| A | LYS559 |
| A | TYR560 |
| A | ASN561 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"23251397","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22673905","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"21892188","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23251397","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22673905","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"21892188","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23251397","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22673905","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23251397","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30472116","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9QYM2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Sterically intereferes with binding of internal ADP-D-ribose moieties of poly(ADP-ribose) to preferntially bind terminal moieties and drive exo-glycohydrolitic action","evidences":[{"source":"PubMed","id":"23917065","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






