Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004725 | molecular_function | protein tyrosine phosphatase activity |
A | 0006470 | biological_process | protein dephosphorylation |
A | 0016311 | biological_process | dephosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue MG A 301 |
Chain | Residue |
A | HOH418 |
A | HOH478 |
A | HOH607 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue CL A 302 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue GOL A 303 |
Chain | Residue |
A | HOH525 |
A | HOH544 |
A | PRO89 |
A | MET133 |
A | PHE135 |
A | HOH445 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue CL A 304 |
Chain | Residue |
A | ARG112 |
A | VAL113 |
A | HIS175 |
A | HOH520 |
A | HOH646 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP181 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | SER215 | |
A | GLN262 | |
Chain | Residue | Details |
A | TYR20 | |
Chain | Residue | Details |
A | SER50 | |
Chain | Residue | Details |
A | TYR66 | |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: S-nitrosocysteine; in reversibly inhibited form => ECO:0000269|PubMed:22169477 |
Chain | Residue | Details |
A | SER215 | |
Chain | Residue | Details |
A | SER242 | |
A | SER243 | |
Chain | Residue | Details |
A | SER215 | |
A | SER216 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 469 |
Chain | Residue | Details |
A | ASP181 | proton shuttle (general acid/base) |
A | SER215 | covalent catalysis |
A | ARG221 | activator, electrostatic stabiliser |
A | SER222 | activator, electrostatic stabiliser |
A | GLN262 | steric role |