4J5S
TARG1 (C6orf130), Terminal ADP-ribose Glycohydrolase 1 ADP-ribose complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001883 | molecular_function | purine nucleoside binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| 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 | 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 | 0005634 | cellular_component | nucleus |
| 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 | 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 |
| C | 0001883 | molecular_function | purine nucleoside binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005654 | cellular_component | nucleoplasm |
| C | 0005694 | cellular_component | chromosome |
| C | 0005730 | cellular_component | nucleolus |
| C | 0006974 | biological_process | DNA damage response |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0042278 | biological_process | purine nucleoside metabolic process |
| C | 0051725 | biological_process | protein de-ADP-ribosylation |
| C | 0061463 | molecular_function | O-acetyl-ADP-ribose deacetylase activity |
| C | 0090734 | cellular_component | site of DNA damage |
| C | 0140291 | biological_process | peptidyl-glutamate ADP-deribosylation |
| C | 0140293 | molecular_function | ADP-ribosylglutamate hydrolase activity |
| D | 0001883 | molecular_function | purine nucleoside binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005654 | cellular_component | nucleoplasm |
| D | 0005694 | cellular_component | chromosome |
| D | 0005730 | cellular_component | nucleolus |
| D | 0006974 | biological_process | DNA damage response |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0042278 | biological_process | purine nucleoside metabolic process |
| D | 0051725 | biological_process | protein de-ADP-ribosylation |
| D | 0061463 | molecular_function | O-acetyl-ADP-ribose deacetylase activity |
| D | 0090734 | cellular_component | site of DNA damage |
| D | 0140291 | biological_process | peptidyl-glutamate ADP-deribosylation |
| D | 0140293 | molecular_function | ADP-ribosylglutamate hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ZZC A 201 |
| Chain | Residue |
| A | ASP23 |
| A | GLY124 |
| A | CYS125 |
| A | GLY126 |
| A | LEU127 |
| A | ASP128 |
| A | LEU155 |
| A | BO4202 |
| A | HOH307 |
| A | HOH310 |
| A | HOH315 |
| A | LEU24 |
| A | HOH342 |
| A | HOH352 |
| A | HOH465 |
| A | HOH487 |
| A | HOH489 |
| A | HOH491 |
| A | CYS36 |
| A | ILE37 |
| A | GLY46 |
| A | ILE47 |
| A | LYS87 |
| A | PRO121 |
| A | ARG122 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BO4 A 202 |
| Chain | Residue |
| A | ZZC201 |
| A | HOH317 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 203 |
| Chain | Residue |
| A | SER38 |
| A | ARG42 |
| A | MET43 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 204 |
| Chain | Residue |
| A | GLU39 |
| A | CYS41 |
| A | LEU61 |
| A | GLN65 |
| A | LYS66 |
| A | HOH386 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 205 |
| Chain | Residue |
| A | PHE25 |
| A | CYS27 |
| A | PRO28 |
| A | LYS29 |
| A | LYS54 |
| A | ARG79 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 206 |
| Chain | Residue |
| A | GLY78 |
| A | ARG79 |
| A | TYR80 |
| A | ASN113 |
| A | GLY114 |
| A | HOH308 |
| A | HOH327 |
| A | HOH351 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 207 |
| Chain | Residue |
| A | ASN134 |
| A | ALA137 |
| A | HOH340 |
| A | HOH475 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 208 |
| Chain | Residue |
| A | LYS53 |
| A | LYS54 |
| A | HOH427 |
| B | CYS27 |
| B | PRO28 |
| B | LYS29 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 209 |
| Chain | Residue |
| A | PRO28 |
| A | ASP31 |
| A | HOH316 |
| A | HOH328 |
| A | HOH363 |
| A | HOH387 |
| A | HOH517 |
| C | LYS52 |
| site_id | BC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ZZC B 201 |
| Chain | Residue |
| B | ASP23 |
| B | LEU24 |
| B | CYS36 |
| B | ILE37 |
| B | SER38 |
| B | GLY46 |
| B | ILE47 |
| B | THR86 |
| B | LYS87 |
| B | ALA90 |
| B | PRO121 |
| B | ARG122 |
| B | GLY124 |
| B | CYS125 |
| B | GLY126 |
| B | LEU127 |
| B | ASP128 |
| B | LEU155 |
| B | SBE202 |
| B | HOH309 |
| B | HOH314 |
| B | HOH318 |
| B | HOH374 |
| B | HOH426 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SBE B 202 |
| Chain | Residue |
| B | ARG122 |
| B | ZZC201 |
| B | HOH358 |
| B | HOH454 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 203 |
| Chain | Residue |
| B | HOH374 |
| B | SER38 |
| B | ARG42 |
| B | MET43 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 204 |
| Chain | Residue |
| B | PHE25 |
| B | CYS27 |
| B | PRO28 |
| B | LYS29 |
| B | LYS54 |
| B | ARG79 |
| B | HOH416 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 205 |
| Chain | Residue |
| B | PRO28 |
| B | ASP31 |
| B | SER119 |
| B | THR151 |
| B | TYR153 |
| B | HOH323 |
| B | HOH412 |
| B | HOH441 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 206 |
| Chain | Residue |
| B | GLY114 |
| B | HOH422 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 207 |
| Chain | Residue |
| B | LYS66 |
| B | VAL71 |
| B | VAL73 |
| B | HOH317 |
| B | HOH320 |
| B | HOH370 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 208 |
| Chain | Residue |
| B | GLU39 |
| B | CYS41 |
| B | LEU61 |
| B | GLN65 |
| B | LYS66 |
| B | HOH359 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 209 |
| Chain | Residue |
| B | THR95 |
| B | TYR96 |
| B | GLU97 |
| site_id | CC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO B 210 |
| Chain | Residue |
| B | ASN134 |
| site_id | CC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ZZC C 201 |
| Chain | Residue |
| C | ASP23 |
| C | LEU24 |
| C | CYS36 |
| C | ILE37 |
| C | GLY46 |
| C | ILE47 |
| C | LYS87 |
| C | ALA90 |
| C | PRO121 |
| C | ARG122 |
| C | GLY124 |
| C | CYS125 |
| C | GLY126 |
| C | LEU127 |
| C | ASP128 |
| C | TYR153 |
| C | HOH315 |
| C | HOH316 |
| C | HOH318 |
| C | HOH370 |
| C | HOH375 |
| C | HOH399 |
| C | HOH411 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 202 |
| Chain | Residue |
| C | SER38 |
| C | ARG42 |
| C | MET43 |
| site_id | CC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO C 203 |
| Chain | Residue |
| C | PHE25 |
| C | CYS27 |
| C | PRO28 |
| C | LYS29 |
| C | LYS54 |
| C | ARG79 |
| C | HOH373 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 204 |
| Chain | Residue |
| C | GLU39 |
| C | CYS41 |
| C | LEU61 |
| C | GLN65 |
| C | LYS66 |
| C | HOH354 |
| site_id | CC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ZZC D 201 |
| Chain | Residue |
| D | ASP23 |
| D | LEU24 |
| D | CYS36 |
| D | ILE37 |
| D | GLY46 |
| D | ILE47 |
| D | LYS87 |
| D | ALA90 |
| D | PRO121 |
| D | ARG122 |
| D | GLY124 |
| D | CYS125 |
| D | GLY126 |
| D | LEU127 |
| D | ASP128 |
| D | TYR153 |
| D | HOH309 |
| D | HOH310 |
| D | HOH314 |
| D | HOH331 |
| D | HOH380 |
| D | HOH388 |
| D | HOH411 |
| D | HOH413 |
| D | HOH437 |
| site_id | CC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL D 202 |
| Chain | Residue |
| D | SER38 |
| D | ARG42 |
| D | MET43 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 203 |
| Chain | Residue |
| D | CYS27 |
| D | PRO28 |
| D | LYS29 |
| D | LYS54 |
| D | ARG79 |
| site_id | CC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 204 |
| Chain | Residue |
| D | GLU39 |
| D | CYS41 |
| D | LEU61 |
| D | GLN65 |
| D | LYS66 |
| D | HOH358 |
| site_id | DC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 205 |
| Chain | Residue |
| D | GLY78 |
| D | ARG79 |
| D | TYR80 |
| D | ASN113 |
| D | GLY114 |
| D | HOH306 |
| D | HOH323 |
| site_id | DC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 206 |
| Chain | Residue |
| D | LYS66 |
| D | VAL71 |
| D | VAL73 |
| D | HOH320 |
| D | HOH337 |
| D | HOH417 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:23481255 |
| Chain | Residue | Details |
| A | LYS87 | |
| B | LYS87 | |
| C | LYS87 | |
| D | LYS87 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:21849506, ECO:0000269|PubMed:23481255 |
| Chain | Residue | Details |
| A | ASP128 | |
| B | ASP128 | |
| C | ASP128 | |
| D | ASP128 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21849506 |
| Chain | Residue | Details |
| A | LEU24 | |
| B | LEU24 | |
| C | LEU24 | |
| D | LEU24 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21849506, ECO:0000269|PubMed:23481255 |
| Chain | Residue | Details |
| A | ARG122 | |
| A | LEU155 | |
| B | ARG122 | |
| B | LEU155 | |
| C | ARG122 | |
| C | LEU155 | |
| D | ARG122 | |
| D | LEU155 |
