Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
| A | 0006470 | biological_process | protein dephosphorylation |
| A | 0043169 | molecular_function | cation binding |
| B | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
| B | 0006470 | biological_process | protein dephosphorylation |
| B | 0043169 | molecular_function | cation binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 306 |
| Chain | Residue |
| A | ASP60 |
| A | OCS242 |
| A | ASP243 |
| A | ASP286 |
| A | HOH307 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 306 |
| Chain | Residue |
| B | HOH334 |
| B | HOH355 |
| B | ASP60 |
| B | OCS242 |
| B | ASP243 |
| B | ASP286 |
Functional Information from PROSITE/UniProt
| site_id | PS01032 |
| Number of Residues | 9 |
| Details | PPM_1 PPM-type phosphatase domain signature. FFAVYDGHA |
| Chain | Residue | Details |
| A | PHE55-ALA63 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18058037","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2P8E","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)"} |
