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 | ACT_SITE: Phosphocysteine intermediate |
Chain | Residue | Details |
A | SER403 | |
B | SER403 | |
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 |