5Y16
Crystal structure of human DUSP28(Y102H)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| A | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
| A | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| A | 0006470 | biological_process | protein dephosphorylation |
| A | 0016311 | biological_process | dephosphorylation |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0017018 | molecular_function | myosin phosphatase activity |
| B | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| B | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
| B | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| B | 0006470 | biological_process | protein dephosphorylation |
| B | 0016311 | biological_process | dephosphorylation |
| B | 0016791 | molecular_function | phosphatase activity |
| B | 0017018 | molecular_function | myosin phosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 A 201 |
| Chain | Residue |
| A | ASP72 |
| A | SER103 |
| A | LYS104 |
| A | ASN105 |
| A | GLY106 |
| A | ARG107 |
| A | SER108 |
| A | ARG109 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 202 |
| Chain | Residue |
| A | ARG53 |
| A | GLN54 |
| A | PHE71 |
| A | ARG109 |
| A | SER52 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 B 201 |
| Chain | Residue |
| B | ASP72 |
| B | SER103 |
| B | LYS104 |
| B | ASN105 |
| B | GLY106 |
| B | ARG107 |
| B | SER108 |
| B | ARG109 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 202 |
| Chain | Residue |
| B | LYS134 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000305|PubMed:29121083 |
| Chain | Residue | Details |
| A | SER103 | |
| B | SER103 |
