4EPP
Canonical poly(ADP-ribose) glycohydrolase from Tetrahymena thermophila.
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 |
| B | 0004649 | molecular_function | poly(ADP-ribose) glycohydrolase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006282 | biological_process | regulation of DNA repair |
| B | 0009225 | biological_process | nucleotide-sugar metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0072570 | molecular_function | ADP-D-ribose binding |
| B | 0140292 | molecular_function | ADP-ribosylserine hydrolase activity |
| B | 1990966 | biological_process | ATP generation from poly-ADP-D-ribose |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE APR A 501 |
| Chain | Residue |
| A | LEU226 |
| A | GLU256 |
| A | TYR296 |
| A | LYS365 |
| A | GLY367 |
| A | CYS368 |
| A | GLY369 |
| A | ALA370 |
| A | PHE371 |
| A | CYS396 |
| A | PHE398 |
| A | ILE227 |
| A | HOH603 |
| A | HOH604 |
| A | HOH614 |
| A | HOH677 |
| A | HOH817 |
| A | HOH837 |
| A | HOH840 |
| A | HOH846 |
| A | GLU228 |
| A | PHE238 |
| A | ASN240 |
| A | GLY245 |
| A | VAL253 |
| A | GLN254 |
| A | GLU255 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE APR B 501 |
| Chain | Residue |
| B | LEU226 |
| B | ILE227 |
| B | GLU228 |
| B | PHE238 |
| B | ASN240 |
| B | GLY245 |
| B | VAL253 |
| B | GLN254 |
| B | GLU255 |
| B | GLU256 |
| B | TYR293 |
| B | TYR296 |
| B | LYS365 |
| B | GLY367 |
| B | CYS368 |
| B | GLY369 |
| B | ALA370 |
| B | PHE371 |
| B | PHE398 |
| B | HOH605 |
| B | HOH606 |
| B | HOH610 |
| B | HOH676 |
| B | HOH677 |
| B | HOH771 |
| B | HOH785 |
| B | HOH855 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 234 |
| Details | Domain: {"description":"PARG helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 382 |
| Details | Domain: {"description":"PARG catalytic Macro","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| 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 | 2 |
| 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 | 2 |
| 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 | 20 |
| 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 | 4 |
| 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 | 2 |
| 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 |
