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 PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue MG A 401 |
Chain | Residue |
A | THR62 |
A | ASP63 |
A | ASP64 |
A | ASP305 |
A | HOH523 |
A | HOH742 |
site_id | AC2 |
Number of Residues | 15 |
Details | binding site for residue CIT A 402 |
Chain | Residue |
A | GLY103 |
A | ALA104 |
A | GLY136 |
A | ASN137 |
A | GLY138 |
A | MET141 |
A | HIS168 |
A | ILE260 |
A | HOH508 |
A | HOH521 |
A | HOH547 |
B | GLU33 |
A | ASP63 |
A | GLY101 |
A | TYR102 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue ACT A 403 |
Chain | Residue |
A | TYR118 |
A | SER119 |
A | ASP120 |
A | HOH545 |
A | HOH776 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue ACT A 404 |
Chain | Residue |
A | GLU51 |
A | LEU286 |
A | GLN291 |
A | HOH512 |
A | HOH567 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue ACT A 405 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue ACT A 406 |
Chain | Residue |
A | MET9 |
A | GLN14 |
A | LEU188 |
A | GLN189 |
A | HOH728 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue GOL A 407 |
Chain | Residue |
A | GLU191 |
A | TYR318 |
A | TYR319 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue GOL A 408 |
Chain | Residue |
A | ALA37 |
A | VAL38 |
A | SER299 |
A | LEU300 |
A | GLY301 |
A | HOH504 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue GOL A 409 |
Chain | Residue |
A | GLN108 |
A | LYS111 |
B | GLU31 |
B | PHE46 |
B | LEU49 |
B | LEU50 |
B | THR58 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue GOL A 410 |
Chain | Residue |
A | ASP80 |
A | ASP155 |
A | PHE159 |
A | GLN352 |
A | HOH529 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue MG B 401 |
Chain | Residue |
B | THR62 |
B | ASP63 |
B | ASP64 |
B | ASP305 |
B | HOH554 |
B | HOH735 |
site_id | AD3 |
Number of Residues | 15 |
Details | binding site for residue CIT B 402 |
Chain | Residue |
A | GLU33 |
B | ASP63 |
B | GLY101 |
B | TYR102 |
B | GLY103 |
B | ALA104 |
B | GLY136 |
B | ASN137 |
B | GLY138 |
B | MET141 |
B | HIS168 |
B | ILE260 |
B | HOH505 |
B | HOH518 |
B | HOH548 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue ACT B 403 |
Chain | Residue |
B | PHE122 |
B | ARG126 |
B | GLN165 |
B | HOH704 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue ACT B 404 |
Chain | Residue |
B | GLU51 |
B | LEU286 |
B | GLN291 |
B | HOH527 |
B | HOH597 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue ACT B 405 |
Chain | Residue |
B | ASN288 |
B | ASP322 |
B | HOH726 |
site_id | AD7 |
Number of Residues | 8 |
Details | binding site for residue GOL B 406 |
Chain | Residue |
B | HOH713 |
B | ALA37 |
B | VAL38 |
B | ALA250 |
B | SER299 |
B | LEU300 |
B | GLY301 |
B | HOH502 |
site_id | AD8 |
Number of Residues | 9 |
Details | binding site for residue GOL B 407 |
Chain | Residue |
A | SER35 |
A | ASP36 |
A | HOH522 |
B | PHE129 |
B | SER134 |
B | TYR135 |
B | GLY136 |
B | ILE260 |
B | ALA261 |
site_id | AD9 |
Number of Residues | 8 |
Details | binding site for residue GOL B 408 |
Chain | Residue |
A | GLU31 |
A | PHE46 |
A | LEU49 |
A | LEU50 |
A | THR58 |
B | GLN108 |
B | LYS111 |
B | HOH637 |
site_id | AE1 |
Number of Residues | 6 |
Details | binding site for residue GOL B 409 |
Chain | Residue |
B | ARG126 |
B | GLY131 |
B | LYS132 |
B | GLY133 |
B | ALA169 |
B | HOH564 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP26 | |
B | ASP26 | |
Chain | Residue | Details |
B | ASP303 | |
B | ASP305 | |
A | GLU33 | |
A | ASP64 | |
A | ASP303 | |
A | ASP305 | |
B | GLU33 | |
B | ASP64 | |
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 | |
Chain | Residue | Details |
A | GLU33 | |
B | GLU33 | |