4J5R
TARG1 (C6orf130), Terminal ADP-ribose Glycohydrolase 1 bound to ADP-HPD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001883 | molecular_function | purine nucleoside binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005694 | cellular_component | chromosome |
| A | 0005730 | cellular_component | nucleolus |
| A | 0006974 | biological_process | DNA damage response |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042278 | biological_process | purine nucleoside metabolic process |
| A | 0047407 | molecular_function | ADP-ribosyl-[dinitrogen reductase] hydrolase activity |
| A | 0051725 | biological_process | protein de-ADP-ribosylation |
| A | 0061463 | molecular_function | O-acetyl-ADP-ribose deacetylase activity |
| A | 0090734 | cellular_component | site of DNA damage |
| A | 0140291 | biological_process | peptidyl-glutamate ADP-deribosylation |
| A | 0140293 | molecular_function | ADP-ribosylglutamate hydrolase activity |
| B | 0001883 | molecular_function | purine nucleoside binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005694 | cellular_component | chromosome |
| B | 0005730 | cellular_component | nucleolus |
| B | 0006974 | biological_process | DNA damage response |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042278 | biological_process | purine nucleoside metabolic process |
| B | 0047407 | molecular_function | ADP-ribosyl-[dinitrogen reductase] hydrolase activity |
| B | 0051725 | biological_process | protein de-ADP-ribosylation |
| B | 0061463 | molecular_function | O-acetyl-ADP-ribose deacetylase activity |
| B | 0090734 | cellular_component | site of DNA damage |
| B | 0140291 | biological_process | peptidyl-glutamate ADP-deribosylation |
| B | 0140293 | molecular_function | ADP-ribosylglutamate hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE A1R A 201 |
| Chain | Residue |
| A | CYS33 |
| A | ARG119 |
| A | GLY121 |
| A | CYS122 |
| A | GLY123 |
| A | LEU124 |
| A | ASP125 |
| A | TYR150 |
| A | LEU152 |
| A | CL202 |
| A | HOH306 |
| A | MET40 |
| A | HOH313 |
| A | HOH317 |
| A | HOH371 |
| A | HOH390 |
| A | HOH391 |
| A | HOH459 |
| A | HOH460 |
| A | HOH465 |
| A | HOH475 |
| A | HOH478 |
| A | ALA42 |
| A | HOH512 |
| A | HOH518 |
| A | HOH587 |
| B | GLU138 |
| B | HOH304 |
| B | HOH323 |
| A | GLY43 |
| A | ILE44 |
| A | ALA45 |
| A | LEU47 |
| A | LYS84 |
| A | PRO118 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 202 |
| Chain | Residue |
| A | SER35 |
| A | ARG39 |
| A | MET40 |
| A | A1R201 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 203 |
| Chain | Residue |
| A | GLU57 |
| B | GLU57 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 204 |
| Chain | Residue |
| A | GLU36 |
| A | CYS38 |
| A | LEU58 |
| A | GLN62 |
| A | LYS63 |
| A | HOH363 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 205 |
| Chain | Residue |
| A | PHE22 |
| A | CYS24 |
| A | PRO25 |
| A | LYS26 |
| A | LYS51 |
| A | ARG76 |
| A | HOH542 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE EDO A 206 |
| Chain | Residue |
| A | GLN97 |
| A | LYS98 |
| A | GLU101 |
| A | HOH351 |
| A | HOH354 |
| A | HOH355 |
| A | HOH404 |
| A | HOH441 |
| A | HOH588 |
| A | HOH608 |
| B | HOH493 |
| site_id | AC7 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE A1R B 201 |
| Chain | Residue |
| A | GLU138 |
| A | HOH302 |
| A | HOH314 |
| B | LEU21 |
| B | CYS33 |
| B | MET40 |
| B | ALA42 |
| B | GLY43 |
| B | ILE44 |
| B | ALA45 |
| B | LEU47 |
| B | LYS84 |
| B | PRO118 |
| B | ARG119 |
| B | GLY121 |
| B | CYS122 |
| B | GLY123 |
| B | LEU124 |
| B | ASP125 |
| B | CL202 |
| B | HOH306 |
| B | HOH331 |
| B | HOH363 |
| B | HOH389 |
| B | HOH420 |
| B | HOH427 |
| B | HOH460 |
| B | HOH462 |
| B | HOH466 |
| B | HOH492 |
| B | HOH493 |
| B | HOH518 |
| B | HOH580 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 202 |
| Chain | Residue |
| B | ARG39 |
| B | MET40 |
| B | A1R201 |
| B | SER35 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 203 |
| Chain | Residue |
| B | GLU36 |
| B | CYS38 |
| B | LEU58 |
| B | GLN62 |
| B | LYS63 |
| B | HOH467 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 204 |
| Chain | Residue |
| B | TYR77 |
| B | ASN110 |
| B | HOH393 |
| B | HOH396 |
| B | HOH499 |
| B | HOH545 |
| B | HOH583 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 205 |
| Chain | Residue |
| B | PHE22 |
| B | CYS24 |
| B | PRO25 |
| B | LYS51 |
| B | ARG76 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 206 |
| Chain | Residue |
| A | PRO91 |
| B | HOH456 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"23481255","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"21849506","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23481255","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21849506","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21849506","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23481255","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
