6G1Q
ADP-ribosylserine hydrolase ARH3 of Latimeria chalumnae in complex with ADP-ribose
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 | 0060546 | biological_process | negative regulation of necroptotic process |
| A | 0140290 | biological_process | peptidyl-serine ADP-deribosylation |
| A | 0140292 | molecular_function | ADP-ribosylserine hydrolase activity |
| 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 | 0060546 | biological_process | negative regulation of necroptotic process |
| B | 0140290 | biological_process | peptidyl-serine ADP-deribosylation |
| B | 0140292 | molecular_function | ADP-ribosylserine hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | THR62 |
| A | ASP63 |
| A | ASP64 |
| A | ASP305 |
| A | AR6402 |
| A | HOH501 |
| A | HOH519 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | binding site for residue AR6 A 402 |
| Chain | Residue |
| A | ASP64 |
| A | GLY101 |
| A | GLY103 |
| A | ALA104 |
| A | GLY105 |
| A | VAL106 |
| A | PHE129 |
| A | GLY133 |
| A | SER134 |
| A | TYR135 |
| A | GLY136 |
| A | ASN137 |
| A | GLY138 |
| A | HIS168 |
| A | ILE260 |
| A | ASP303 |
| A | ASP305 |
| A | THR306 |
| A | MG401 |
| A | HOH501 |
| A | HOH503 |
| A | HOH509 |
| B | ALA37 |
| B | ASP42 |
| A | GLU33 |
| A | ASP63 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 401 |
| Chain | Residue |
| B | THR62 |
| B | ASP63 |
| B | ASP64 |
| B | ASP305 |
| B | AR6402 |
| B | HOH525 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | binding site for residue AR6 B 402 |
| Chain | Residue |
| A | ASP42 |
| B | GLU33 |
| B | ASP63 |
| B | ASP64 |
| B | GLY101 |
| B | GLY103 |
| B | ALA104 |
| B | GLY105 |
| B | VAL106 |
| B | PHE129 |
| B | GLY133 |
| B | SER134 |
| B | TYR135 |
| B | GLY136 |
| B | ASN137 |
| B | GLY138 |
| B | HIS168 |
| B | ILE260 |
| B | ASP303 |
| B | ASP305 |
| B | THR306 |
| B | MG401 |
| B | HOH501 |
| B | HOH525 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"34321462","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7AQM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30472116","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34321462","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7AQM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30472116","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Glutamate flap","evidences":[{"source":"UniProtKB","id":"Q9NX46","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
