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 | 6 |
Details | binding site for residue MG A 401 |
Chain | Residue |
A | ASP118 |
A | ASP306 |
A | ASP368 |
A | HOH509 |
A | HOH518 |
C | HOH412 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MG A 402 |
Chain | Residue |
A | HOH517 |
C | HOH414 |
A | ASP118 |
A | GLY119 |
A | HOH509 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue MG B 401 |
Chain | Residue |
B | ASP118 |
B | ASP306 |
B | ASP368 |
B | HOH517 |
B | HOH531 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue MG B 402 |
Chain | Residue |
B | ASP75 |
B | ASP118 |
B | GLY119 |
B | HOH502 |
B | HOH517 |
site_id | AC5 |
Number of Residues | 14 |
Details | binding site for residue PYV C 301 |
Chain | Residue |
C | LYS76 |
C | PHE78 |
C | VAL79 |
C | PRO103 |
C | SER107 |
C | GLU109 |
C | PHE125 |
C | HIS130 |
C | LEU132 |
C | TYR135 |
C | LEU179 |
C | ASN182 |
C | HOH404 |
C | HOH417 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue SO4 C 302 |
Chain | Residue |
C | SER100 |
C | GLY101 |
C | HOH402 |
C | HOH403 |
C | HOH412 |
C | HOH414 |
C | HOH421 |
site_id | AC7 |
Number of Residues | 13 |
Details | binding site for residue PYV D 301 |
Chain | Residue |
D | LYS76 |
D | PHE78 |
D | VAL79 |
D | PRO103 |
D | SER107 |
D | PHE125 |
D | HIS130 |
D | LEU132 |
D | TYR135 |
D | LEU178 |
D | LEU179 |
D | ASN182 |
D | HOH409 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue SO4 D 302 |
Chain | Residue |
B | ASP368 |
B | HOH502 |
B | HOH517 |
D | GLY101 |
D | HOH405 |
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 |
C | LYS76 | |
D | LYS76 | |
A | ASP306 | |
A | ASP368 | |
B | ASP118 | |
B | GLY119 | |
B | ASP306 | |
B | ASP368 | |
Chain | Residue | Details |
C | ALA104 | |
C | ARG131 | |
C | GLU156 | |
D | ALA104 | |
D | ARG131 | |
D | GLU156 | |
Chain | Residue | Details |
C | PRO77 | |
C | VAL175 | |
D | PRO77 | |
D | VAL175 | |
Chain | Residue | Details |
C | PRO103 | |
C | THR167 | |
D | PRO103 | |
D | THR167 | |