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 | 3 |
Details | BINDING SITE FOR RESIDUE CL A 799 |
Chain | Residue |
A | ARG524 |
A | ARG754 |
A | GLN762 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 799 |
Chain | Residue |
B | ARG524 |
B | ARG754 |
B | GLN762 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE 073 A 401 |
Chain | Residue |
A | ASP548 |
A | LEU619 |
A | PHE682 |
A | CYS715 |
A | SER716 |
A | ALA717 |
A | GLY718 |
A | ILE719 |
A | GLY720 |
A | ARG721 |
A | GLN762 |
B | GLY514 |
B | ALA518 |
B | GLN521 |
A | HOH44 |
A | TYR546 |
A | ARG547 |
site_id | AC4 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE 073 B 402 |
Chain | Residue |
A | ALA518 |
A | ASP522 |
A | HIS525 |
A | GLU526 |
B | HOH115 |
B | TYR546 |
B | ARG547 |
B | ASP548 |
B | SER618 |
B | LEU619 |
B | PHE682 |
B | CYS715 |
B | SER716 |
B | ALA717 |
B | GLY718 |
B | ILE719 |
B | GLY720 |
B | ARG721 |
B | MET758 |
B | GLN762 |
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 | VAL713-GLY723 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Phosphocysteine intermediate |
Chain | Residue | Details |
A | CYS715 | |
B | CYS715 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP681 | |
B | ASP681 | |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | CYS715 | |
A | GLN762 | |
B | CYS715 | |
B | GLN762 | |
Chain | Residue | Details |
A | MET501 | |
B | MET501 | |
Chain | Residue | Details |
A | TYR520 | |
B | TYR520 | |
Chain | Residue | Details |
A | SER550 | |
B | SER550 | |
Chain | Residue | Details |
A | TYR566 | |
B | TYR566 | |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: S-nitrosocysteine; in reversibly inhibited form => ECO:0000269|PubMed:22169477 |
Chain | Residue | Details |
A | CYS715 | |
B | CYS715 | |
Chain | Residue | Details |
A | SER742 | |
A | SER743 | |
B | SER742 | |
B | SER743 | |
Chain | Residue | Details |
A | CYS715 | |
A | SER716 | |
B | CYS715 | |
B | SER716 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1d5r |
Chain | Residue | Details |
A | ARG721 | |
A | CYS715 | |
A | ASP681 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1d5r |
Chain | Residue | Details |
B | ARG721 | |
B | CYS715 | |
B | ASP681 | |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1d5r |
Chain | Residue | Details |
A | ARG721 | |
A | SER722 | |
A | CYS715 | |
A | ASP681 | |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1d5r |
Chain | Residue | Details |
B | ARG721 | |
B | SER722 | |
B | CYS715 | |
B | ASP681 | |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 469 |
Chain | Residue | Details |
A | ASP681 | proton shuttle (general acid/base) |
A | CYS715 | covalent catalysis |
A | ARG721 | activator, electrostatic stabiliser |
A | SER722 | activator, electrostatic stabiliser |
A | GLN762 | steric role |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 469 |
Chain | Residue | Details |
B | ASP681 | proton shuttle (general acid/base) |
B | CYS715 | covalent catalysis |
B | ARG721 | activator, electrostatic stabiliser |
B | SER722 | activator, electrostatic stabiliser |
B | GLN762 | steric role |