4L2H
Structure of a catalytically inactive PARG in complex with a poly-ADP-ribose fragment
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004649 | molecular_function | poly(ADP-ribose) glycohydrolase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006282 | biological_process | regulation of DNA repair |
| A | 0009225 | biological_process | nucleotide-sugar metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0072570 | molecular_function | ADP-D-ribose binding |
| A | 0140292 | molecular_function | ADP-ribosylserine hydrolase activity |
| A | 1990966 | biological_process | ATP generation from poly-ADP-D-ribose |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR LINKED RESIDUES A 700 to 701 |
| Chain | Residue |
| A | ARG164 |
| A | ASN250 |
| A | GLY251 |
| A | LEU252 |
| A | VAL253 |
| A | GLN254 |
| A | GLU255 |
| A | GLN256 |
| A | TYR296 |
| A | SER297 |
| A | LYS365 |
| A | LEU226 |
| A | GLY367 |
| A | CYS368 |
| A | GLY369 |
| A | ALA370 |
| A | PHE371 |
| A | PHE398 |
| A | HOH815 |
| A | HOH825 |
| A | HOH827 |
| A | HOH835 |
| A | ILE227 |
| A | HOH888 |
| A | HOH930 |
| A | HOH1048 |
| A | HOH1051 |
| A | HOH1075 |
| A | HOH1120 |
| A | HOH1143 |
| A | HOH1149 |
| A | HOH1259 |
| A | GLU228 |
| A | PHE238 |
| A | ASN240 |
| A | GLY245 |
| A | GLY246 |
| A | GLY249 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 117 |
| Details | Domain: {"description":"PARG helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 191 |
| Details | Domain: {"description":"PARG catalytic Macro","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"22673905","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EPP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"22673905","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23917065","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EPP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L2H","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"22673905","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23917065","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EPP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L2H","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22673905","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23917065","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EPP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L2H","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23917065","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L2H","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Site: {"description":"Sterically interferes with binding of internal ADP-D-ribose moieties of poly(ADP-ribose) to preferentially bind terminal moieties and drive exo-glycohydrolitic activity","evidences":[{"source":"PubMed","id":"23917065","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
