Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
| A | 0006470 | biological_process | protein dephosphorylation |
| A | 0043169 | molecular_function | cation binding |
| B | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
| B | 0006470 | biological_process | protein dephosphorylation |
| B | 0043169 | molecular_function | cation binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | ASP220 |
| A | LYS239 |
| A | ASP306 |
| A | ASP310 |
| A | HOH505 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | HOH516 |
| A | HOH518 |
| A | ASP118 |
| A | GLY119 |
| A | MG403 |
| A | HOH511 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | ASP118 |
| A | ASP306 |
| A | ASP368 |
| A | MG402 |
| A | HOH501 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 401 |
| Chain | Residue |
| B | ASP118 |
| B | GLY119 |
| B | MG402 |
| B | HOH502 |
| B | HOH507 |
| B | HOH508 |
| B | HOH509 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | ASP118 |
| B | ASP306 |
| B | ASP368 |
| B | MG401 |
| B | HOH501 |
| B | HOH509 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue A8S C 301 |
| Chain | Residue |
| C | LYS76 |
| C | LEU102 |
| C | SER107 |
| C | PHE125 |
| C | PHE174 |
| C | LEU178 |
| C | ASN182 |
| C | HOH401 |
| C | HOH402 |
| C | HOH404 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue A8S D 301 |
| Chain | Residue |
| D | LYS76 |
| D | LEU102 |
| D | ALA104 |
| D | SER107 |
| D | PHE125 |
| D | HIS130 |
| D | LEU132 |
| D | PHE174 |
| D | LEU178 |
| D | ASN182 |
Functional Information from PROSITE/UniProt
| site_id | PS01032 |
| Number of Residues | 9 |
| Details | PPM_1 PPM-type phosphatase domain signature. LFGVFDGHG |
| Chain | Residue | Details |
| A | LEU113-GLY121 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| B | ASP306 | |
| B | ASP368 | |
| C | LYS76 | |
| D | LYS76 | |
| A | ASP306 | |
| A | ASP368 | |
| B | ASP118 | |
| B | GLY119 | |
| Chain | Residue | Details |
| C | GLU156 | |
| D | ALA104 | |
| D | ARG131 | |
| D | GLU156 | |
| C | ALA104 | |
| C | ARG131 | |
| Chain | Residue | Details |
| C | PRO77 | |
| C | VAL175 | |
| D | PRO77 | |
| D | VAL175 | |
| Chain | Residue | Details |
| C | PRO103 | |
| C | THR167 | |
| D | PRO103 | |
| D | THR167 | |
