Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004427 | molecular_function | inorganic diphosphate phosphatase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006796 | biological_process | phosphate-containing compound metabolic process |
A | 0016311 | biological_process | dephosphorylation |
A | 0016607 | cellular_component | nuclear speck |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016791 | molecular_function | phosphatase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004427 | molecular_function | inorganic diphosphate phosphatase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006796 | biological_process | phosphate-containing compound metabolic process |
B | 0016311 | biological_process | dephosphorylation |
B | 0016607 | cellular_component | nuclear speck |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016791 | molecular_function | phosphatase activity |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE POP A 500 |
Chain | Residue |
A | ASP17 |
A | HOH2183 |
A | HOH2184 |
A | HOH2185 |
A | ILE18 |
A | SER19 |
A | THR54 |
A | ASN55 |
A | GLU56 |
A | LYS189 |
A | MG501 |
A | HOH2053 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 501 |
Chain | Residue |
A | ASP17 |
A | SER19 |
A | ASP214 |
A | POP500 |
A | HOH2139 |
A | HOH2183 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EPE A 502 |
Chain | Residue |
A | LYS155 |
A | MET173 |
A | LYS174 |
A | GLU177 |
A | ALA184 |
A | VAL186 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 503 |
Chain | Residue |
A | LEU165 |
A | ARG239 |
B | GLU144 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE POP B 500 |
Chain | Residue |
B | ASP17 |
B | ILE18 |
B | SER19 |
B | THR54 |
B | ASN55 |
B | GLU56 |
B | LYS189 |
B | MG501 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 501 |
Chain | Residue |
B | ASP17 |
B | SER19 |
B | ASP214 |
B | POP500 |
B | HOH2026 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EPE B 502 |
Chain | Residue |
B | LYS174 |
B | GLU177 |
B | ALA184 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP17 | |
B | ASP214 | |
A | SER19 | |
A | THR54 | |
A | LYS189 | |
A | ASP214 | |
B | ASP17 | |
B | SER19 | |
B | THR54 | |
B | LYS189 | |