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 | 15 |
Details | binding site for residue OTA A 301 |
Chain | Residue |
A | TYR46 |
A | GLY220 |
A | ARG221 |
A | GOL309 |
A | HOH428 |
A | HOH486 |
A | HOH487 |
A | ASP48 |
A | LYS120 |
A | ASP181 |
A | PHE182 |
A | CYS215 |
A | SER216 |
A | ALA217 |
A | ILE219 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue CL A 302 |
Chain | Residue |
A | ARG112 |
A | VAL113 |
A | HIS175 |
A | HOH485 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue CL A 303 |
Chain | Residue |
A | ARG45 |
A | HOH582 |
A | HOH585 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CL A 304 |
Chain | Residue |
A | TYR20 |
A | ARG24 |
A | ARG254 |
A | GLY259 |
A | GLN262 |
A | GOL309 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue CL A 305 |
Chain | Residue |
A | ARG238 |
A | SER243 |
A | VAL244 |
A | ASP245 |
A | GOL311 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue TRS A 306 |
Chain | Residue |
A | HIS54 |
A | HOH483 |
A | HOH576 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue DMS A 307 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue DMS A 308 |
Chain | Residue |
A | PHE196 |
A | ARG199 |
A | GLU200 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue GOL A 309 |
Chain | Residue |
A | ASP48 |
A | MET258 |
A | GLY259 |
A | GLN262 |
A | OTA301 |
A | CL304 |
A | HOH404 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue GOL A 310 |
Chain | Residue |
A | PRO89 |
A | GLN123 |
A | MET133 |
A | HOH468 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue GOL A 311 |
Chain | Residue |
A | GLU76 |
A | ARG238 |
A | LYS248 |
A | GLU252 |
A | CL305 |
A | HOH445 |
A | HOH446 |
A | HOH543 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue GOL A 312 |
Chain | Residue |
A | GLN61 |
A | GLU62 |
A | ASP63 |
A | ASN64 |
A | ASP65 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue GOL A 313 |
Chain | Residue |
A | LYS103 |
A | PRO206 |
A | GLU207 |
A | HIS208 |
A | GLY209 |
A | HOH495 |
A | HOH508 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue GOL A 314 |
Chain | Residue |
A | PRO31 |
A | CYS32 |
A | ARG33 |
A | LYS36 |
A | HOH433 |
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 |