5GTJ
CRYSTAL STRUCTURE OF CATALYTICALLY ACTIVE FORM OF HUMAN DUSP26
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006470 | biological_process | protein dephosphorylation |
A | 0008138 | molecular_function | protein tyrosine/serine/threonine phosphatase activity |
A | 0016311 | biological_process | dephosphorylation |
B | 0006470 | biological_process | protein dephosphorylation |
B | 0008138 | molecular_function | protein tyrosine/serine/threonine phosphatase activity |
B | 0016311 | biological_process | dephosphorylation |
C | 0006470 | biological_process | protein dephosphorylation |
C | 0008138 | molecular_function | protein tyrosine/serine/threonine phosphatase activity |
C | 0016311 | biological_process | dephosphorylation |
D | 0006470 | biological_process | protein dephosphorylation |
D | 0008138 | molecular_function | protein tyrosine/serine/threonine phosphatase activity |
D | 0016311 | biological_process | dephosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue PO4 A 301 |
Chain | Residue |
A | ASP120 |
A | SER152 |
A | ALA153 |
A | VAL154 |
A | GLY155 |
A | VAL156 |
A | SER157 |
A | ARG158 |
A | HOH440 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue PO4 B 301 |
Chain | Residue |
B | ASP120 |
B | SER152 |
B | ALA153 |
B | VAL154 |
B | GLY155 |
B | VAL156 |
B | SER157 |
B | ARG158 |
B | HOH440 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue PO4 C 301 |
Chain | Residue |
C | ASP120 |
C | SER152 |
C | ALA153 |
C | VAL154 |
C | GLY155 |
C | VAL156 |
C | SER157 |
C | ARG158 |
C | HOH467 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue PO4 D 301 |
Chain | Residue |
D | ASP120 |
D | SER152 |
D | ALA153 |
D | VAL154 |
D | GLY155 |
D | VAL156 |
D | SER157 |
D | ARG158 |
D | HOH447 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160 |
Chain | Residue | Details |
A | SER152 | |
B | SER152 | |
C | SER152 | |
D | SER152 |