3HFW
Crystal Structure of human ADP-ribosylhydrolase 1 (hARH1)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003875 | molecular_function | ADP-ribosylarginine hydrolase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005615 | cellular_component | extracellular space |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| A | 0030955 | molecular_function | potassium ion binding |
| A | 0036211 | biological_process | protein modification process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051725 | biological_process | protein de-ADP-ribosylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ADP A 358 |
| Chain | Residue |
| A | LYS85 |
| A | CYS129 |
| A | GLY130 |
| A | HIS163 |
| A | HIS165 |
| A | TYR263 |
| A | SER264 |
| A | SER269 |
| A | SER270 |
| A | HOH383 |
| A | HOH432 |
| A | GLY100 |
| A | GLY101 |
| A | ALA102 |
| A | SER103 |
| A | SER124 |
| A | HIS125 |
| A | GLY127 |
| A | GLY128 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K A 359 |
| Chain | Residue |
| A | TRP24 |
| A | GLU25 |
| A | LEU27 |
| A | HIS299 |
| A | GLY300 |
| A | GLY301 |
| A | SER303 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 360 |
| Chain | Residue |
| A | LEU43 |
| A | SER241 |
| A | HIS294 |
| A | HOH439 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 361 |
| Chain | Residue |
| A | SER54 |
| A | ASP55 |
| A | ASP56 |
| A | ASP304 |
| A | HOH480 |
| A | HOH481 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19407395, ECO:0000269|PubMed:30472116, ECO:0007744|PDB:3HFW |
| Chain | Residue | Details |
| A | SER54 | |
| A | ASP55 | |
| A | ASP56 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:19407395, ECO:0007744|PDB:3HFW |
| Chain | Residue | Details |
| A | LYS85 | |
| A | GLY101 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30472116, ECO:0000305|PubMed:19407395, ECO:0007744|PDB:3HFW |
| Chain | Residue | Details |
| A | SER124 | |
| A | GLY130 | |
| A | HIS163 | |
| A | TYR263 | |
| A | SER269 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30472116 |
| Chain | Residue | Details |
| A | ASP302 | |
| A | ASP304 | |
| A | SER305 |
