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 | 19 |
Details | BINDING SITE FOR CHAIN C OF EPIDERMAL GROWTH FACTOR RECEPTOR DERIVED PEPTIDE |
Chain | Residue |
A | PHE229 |
A | GLY406 |
A | VAL407 |
A | GLY408 |
A | ARG409 |
A | GLN446 |
A | HOH632 |
A | HOH745 |
B | HOH705 |
C | NH2107 |
C | HOH624 |
A | ARG230 |
A | ASP231 |
A | ILE232 |
A | ASP356 |
A | GLN357 |
A | CYS403 |
A | ARG404 |
A | ALA405 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR CHAIN D OF EPIDERMAL GROWTH FACTOR RECEPTOR DERIVED PEPTIDE |
Chain | Residue |
A | ARG278 |
A | ARG295 |
A | LYS342 |
A | THR343 |
A | MET382 |
A | LYS386 |
A | SER388 |
A | SER389 |
A | HOH774 |
B | SER468 |
D | NH27 |
D | HOH539 |
D | HOH540 |
D | HOH542 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR CHAIN E OF EPIDERMAL GROWTH FACTOR RECEPTOR DERIVED PEPTIDE |
Chain | Residue |
A | HOH749 |
B | PHE229 |
B | ARG230 |
B | ASP231 |
B | ILE232 |
B | ASP356 |
B | GLN357 |
B | CYS403 |
B | ARG404 |
B | ALA405 |
B | GLY406 |
B | VAL407 |
B | GLY408 |
B | ARG409 |
B | GLN446 |
E | NH2107 |
E | HOH783 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR CHAIN F OF EPIDERMAL GROWTH FACTOR RECEPTOR DERIVED PEPTIDE |
Chain | Residue |
A | SER468 |
B | ARG278 |
B | ARG295 |
B | LYS342 |
B | THR343 |
B | ILE344 |
B | SER345 |
B | LYS386 |
B | SER388 |
B | SER389 |
B | HOH709 |
F | NH27 |
F | HOH642 |
F | HOH644 |
F | HOH818 |
Functional Information from PROSITE/UniProt
site_id | PS00383 |
Number of Residues | 11 |
Details | TYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. IHCraGvgRTA |
Chain | Residue | Details |
A | ILE401-ALA411 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Phosphocysteine intermediate |
Chain | Residue | Details |
A | CYS403 | |
B | CYS403 | |
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 | CYS403 | |
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 | CYS403 | |
B | ARG409 | |
B | GLU290 | |
B | HIS402 | |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ytw |
Chain | Residue | Details |
A | ASP356 | |
A | THR410 | |
A | CYS403 | |
A | ARG409 | |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ytw |
Chain | Residue | Details |
B | ASP356 | |
B | THR410 | |
B | CYS403 | |
B | ARG409 | |
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 | CYS403 | 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 | CYS403 | nucleofuge, nucleophile |
B | ARG409 | electrostatic stabiliser, hydrogen bond donor |
B | THR410 | electrostatic stabiliser, hydrogen bond donor |