6HOZ
ADP-ribosylserine hydrolase ARH3 of Latimeria chalumnae in complex with inosine diphosphate ribose (IDPr)
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 | 0006974 | biological_process | DNA damage response |
| 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 |
| 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 | 0006281 | biological_process | DNA repair |
| B | 0006974 | biological_process | DNA damage response |
| 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 |
| 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 | R5I403 |
| A | R7I404 |
| A | HOH627 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | ASP305 |
| A | THR306 |
| A | R5I403 |
| A | R7I404 |
| A | GLU33 |
| A | ASP303 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | binding site for residue R5I A 403 |
| Chain | Residue |
| A | GLU33 |
| A | ASP63 |
| 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 | MG402 |
| A | R7I404 |
| A | HOH506 |
| A | HOH514 |
| A | HOH521 |
| A | HOH575 |
| A | HOH597 |
| B | HOH620 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | binding site for residue R7I A 404 |
| Chain | Residue |
| A | GLU33 |
| A | ASP63 |
| A | ASP64 |
| A | GLY101 |
| A | GLY103 |
| 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 | MG402 |
| A | R5I403 |
| A | HOH506 |
| A | HOH510 |
| A | HOH514 |
| A | HOH521 |
| A | HOH575 |
| A | HOH627 |
| B | HOH620 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | ASP80 |
| A | ASP155 |
| A | GLN352 |
| A | HOH570 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | ASN152 |
| A | GLN154 |
| A | ASP155 |
| A | LYS158 |
| A | HOH593 |
| B | GLN123 |
| B | ARG126 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 407 |
| Chain | Residue |
| A | ASN175 |
| A | GLU209 |
| A | PHE231 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 408 |
| Chain | Residue |
| A | GLU337 |
| A | GLU340 |
| B | SER11 |
| B | LEU12 |
| B | ALA13 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 409 |
| Chain | Residue |
| A | GLU97 |
| A | THR99 |
| A | ARG100 |
| A | HOH578 |
| B | THR99 |
| B | HOH528 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue ACT A 410 |
| Chain | Residue |
| A | PHE60 |
| A | HOH502 |
| A | HOH586 |
| A | GLU31 |
| A | THR58 |
| A | LEU59 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 401 |
| Chain | Residue |
| B | THR62 |
| B | ASP63 |
| B | ASP64 |
| B | ASP305 |
| B | R5I403 |
| B | R7I404 |
| B | HOH616 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | GLU33 |
| B | ASP303 |
| B | ASP305 |
| B | THR306 |
| B | R5I403 |
| B | R7I404 |
| site_id | AD4 |
| Number of Residues | 30 |
| Details | binding site for residue R5I B 403 |
| Chain | Residue |
| A | ASP42 |
| A | HOH518 |
| B | GLU33 |
| B | ASP63 |
| B | ASP64 |
| B | GLY101 |
| B | GLY103 |
| 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 | MG402 |
| B | R7I404 |
| B | HOH512 |
| B | HOH526 |
| B | HOH560 |
| B | HOH567 |
| B | HOH587 |
| B | HOH644 |
| site_id | AD5 |
| Number of Residues | 31 |
| Details | binding site for residue R7I B 404 |
| Chain | Residue |
| A | ALA37 |
| A | HOH518 |
| B | GLU33 |
| B | ASP63 |
| B | ASP64 |
| B | GLY101 |
| B | GLY103 |
| 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 | MG402 |
| B | R5I403 |
| B | HOH512 |
| B | HOH524 |
| B | HOH526 |
| B | HOH560 |
| B | HOH567 |
| B | HOH587 |
| B | HOH644 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 405 |
| Chain | Residue |
| B | SER244 |
| B | SER245 |
| B | ASN246 |
| B | HIS275 |
| B | PRO281 |
| B | HOH514 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 406 |
| Chain | Residue |
| B | GLY190 |
| B | GLU191 |
| B | TYR318 |
| B | TYR319 |
| B | HOH534 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 407 |
| Chain | Residue |
| B | ASN175 |
| B | GLU209 |
| B | PHE231 |
| B | HOH627 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 408 |
| Chain | Residue |
| B | ARG126 |
| B | GLN165 |
| B | HOH510 |
| B | HOH569 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 409 |
| Chain | Residue |
| B | GLU97 |
| B | ARG100 |
| B | HOH527 |
| B | HOH528 |
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 |
