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 |
| B | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| B | 0006470 | biological_process | protein dephosphorylation |
| B | 0016311 | biological_process | dephosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR CHAIN C OF HEXAPEPTIDE ASP-ALA-ASP-GLU-PTR-CLE |
| Chain | Residue |
| A | ARG278 |
| A | SER389 |
| C | HOH88 |
| C | HOH90 |
| A | ARG295 |
| A | LYS342 |
| A | THR343 |
| A | SER345 |
| A | MET382 |
| A | TYR383 |
| A | LYS386 |
| A | SER388 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR CHAIN D OF HEXAPEPTIDE ASP-ALA-ASP-GLU-PTR-CLE |
| Chain | Residue |
| A | PHE229 |
| A | ASP356 |
| A | GLN357 |
| A | SER403 |
| A | ARG404 |
| A | ALA405 |
| A | GLY406 |
| A | VAL407 |
| A | GLY408 |
| A | ARG409 |
| A | GLN446 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR CHAIN E OF HEXAPEPTIDE ASP-ALA-ASP-GLU-PTR-CLE |
| Chain | Residue |
| A | SER468 |
| B | ARG278 |
| B | ARG295 |
| B | LYS342 |
| B | THR343 |
| B | SER345 |
| B | MET382 |
| B | TYR383 |
| B | LYS386 |
| B | SER388 |
| B | SER389 |
| E | HOH91 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR CHAIN F OF HEXAPEPTIDE ASP-ALA-ASP-GLU-PTR-CLE |
| Chain | Residue |
| B | PHE229 |
| B | ASP231 |
| B | ASP356 |
| B | GLN357 |
| B | SER403 |
| B | ARG404 |
| B | ALA405 |
| B | GLY406 |
| B | VAL407 |
| B | GLY408 |
| B | ARG409 |
| B | GLN446 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Phosphocysteine intermediate"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1ytw |
| Chain | Residue | Details |
| A | ASP356 | |
| A | THR410 | |
| A | SER403 | |
| A | ARG409 | |
| A | GLU290 | |
| A | HIS402 | |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1ytw |
| Chain | Residue | Details |
| B | ASP356 | |
| B | THR410 | |
| B | SER403 | |
| B | ARG409 | |
| B | GLU290 | |
| B | HIS402 | |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 47 |
| Chain | Residue | Details |
| A | GLU290 | steric role |
| A | TRP354 | steric role |
| A | ASP356 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS402 | electrostatic stabiliser, hydrogen bond donor |
| A | SER403 | nucleofuge, nucleophile |
| A | ARG409 | electrostatic stabiliser, hydrogen bond donor |
| A | THR410 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 47 |
| Chain | Residue | Details |
| B | GLU290 | steric role |
| B | TRP354 | steric role |
| B | ASP356 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS402 | electrostatic stabiliser, hydrogen bond donor |
| B | SER403 | nucleofuge, nucleophile |
| B | ARG409 | electrostatic stabiliser, hydrogen bond donor |
| B | THR410 | electrostatic stabiliser, hydrogen bond donor |
1XXP
