7AQM
ADP-ribosylserine hydrolase ARH3 of Latimeria chalumnae in complex with alpha-1''-O-methyl-ADP-ribose (meADPr)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004649 | molecular_function | poly(ADP-ribose) glycohydrolase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005694 | cellular_component | chromosome |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006281 | biological_process | DNA repair |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0060546 | biological_process | negative regulation of necroptotic process |
| A | 0140290 | biological_process | peptidyl-serine ADP-deribosylation |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004649 | molecular_function | poly(ADP-ribose) glycohydrolase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005694 | cellular_component | chromosome |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006281 | biological_process | DNA repair |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0060546 | biological_process | negative regulation of necroptotic process |
| B | 0140290 | biological_process | peptidyl-serine ADP-deribosylation |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:34321462, ECO:0007744|PDB:7AQM |
| Chain | Residue | Details |
| A | ASP26 | |
| B | ASP26 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30472116, ECO:0000269|PubMed:34321462, ECO:0007744|PDB:7AQM |
| Chain | Residue | Details |
| B | ASP303 | |
| B | ASP305 | |
| A | ASP305 | |
| B | GLU33 | |
| B | ASP64 | |
| A | GLU33 | |
| A | ASP64 | |
| A | ASP303 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30472116 |
| Chain | Residue | Details |
| A | LYS132 | |
| A | HIS168 | |
| A | ILE260 | |
| A | THR306 | |
| B | THR62 | |
| B | ASP63 | |
| B | LYS132 | |
| B | HIS168 | |
| B | ILE260 | |
| B | THR306 | |
| A | THR62 | |
| A | ASP63 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Glutamate flap => ECO:0000250|UniProtKB:Q9NX46 |
| Chain | Residue | Details |
| B | GLU33 | |
| A | GLU33 |
