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 | 4 |
Details | binding site for residue JKV A 401 |
Chain | Residue |
A | ASP29 |
A | PHE30 |
A | PRO31 |
A | GLU170 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue TRS A 402 |
Chain | Residue |
A | HIS54 |
A | LYS128 |
A | GLU129 |
A | GLU130 |
A | HOH584 |
Functional Information from PROSITE/UniProt
site_id | PS00383 |
Number of Residues | 11 |
Details | TYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGigRSG |
Chain | Residue | Details |
A | VAL213-GLY223 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Phosphocysteine intermediate |
Chain | Residue | Details |
A | CYS215 | |
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 | CYS215 | |
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 | CYS215 | |
Chain | Residue | Details |
A | SER242 | |
A | SER243 | |
Chain | Residue | Details |
A | CYS215 | |
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 | CYS215 | covalent catalysis |
A | ARG221 | activator, electrostatic stabiliser |
A | SER222 | activator, electrostatic stabiliser |
A | GLN262 | steric role |