4R30
Structure of human laforin dual specificity phosphatase domain
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 |
| A | 0019203 | molecular_function | carbohydrate phosphatase activity |
| B | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| B | 0006470 | biological_process | protein dephosphorylation |
| B | 0016311 | biological_process | dephosphorylation |
| B | 0019203 | molecular_function | carbohydrate phosphatase activity |
| C | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| C | 0006470 | biological_process | protein dephosphorylation |
| C | 0016311 | biological_process | dephosphorylation |
| C | 0019203 | molecular_function | carbohydrate phosphatase activity |
| D | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| D | 0006470 | biological_process | protein dephosphorylation |
| D | 0016311 | biological_process | dephosphorylation |
| D | 0019203 | molecular_function | carbohydrate phosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 501 |
| Chain | Residue |
| A | SER266 |
| A | ASN267 |
| A | GLY269 |
| A | VAL270 |
| A | GLY271 |
| A | ARG272 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME A 502 |
| Chain | Residue |
| C | ALA254 |
| A | CYS250 |
| A | VAL324 |
| A | HOH636 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME A 503 |
| Chain | Residue |
| A | THR274 |
| A | CYS278 |
| A | LEU289 |
| A | PRO301 |
| A | LEU310 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME A 504 |
| Chain | Residue |
| A | ASN163 |
| A | CYS329 |
| C | TYR294 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 501 |
| Chain | Residue |
| B | SER266 |
| B | ASN267 |
| B | GLY269 |
| B | VAL270 |
| B | GLY271 |
| B | ARG272 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME B 502 |
| Chain | Residue |
| B | CYS250 |
| D | BME502 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME B 503 |
| Chain | Residue |
| B | CYS278 |
| B | LEU289 |
| B | PRO301 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME B 504 |
| Chain | Residue |
| B | ASN163 |
| B | VAL328 |
| B | CYS329 |
| B | LEU331 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 501 |
| Chain | Residue |
| C | SER266 |
| C | ASN267 |
| C | GLY269 |
| C | VAL270 |
| C | GLY271 |
| C | ARG272 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME C 502 |
| Chain | Residue |
| C | CYS250 |
| C | HIS253 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME C 503 |
| Chain | Residue |
| C | THR274 |
| C | CYS278 |
| C | LEU289 |
| C | PRO301 |
| C | LEU310 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME C 504 |
| Chain | Residue |
| A | TYR294 |
| C | VAL328 |
| C | CYS329 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 501 |
| Chain | Residue |
| D | SER266 |
| D | ASN267 |
| D | GLY269 |
| D | VAL270 |
| D | GLY271 |
| D | ARG272 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME D 502 |
| Chain | Residue |
| B | BME502 |
| D | CYS250 |
| D | HIS253 |
| D | ALA254 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME D 503 |
| Chain | Residue |
| D | THR274 |
| D | CYS278 |
| D | LEU289 |
| D | PRO301 |
| D | LEU310 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME D 504 |
| Chain | Residue |
| B | TYR294 |
| D | VAL328 |
| D | CYS329 |
| D | LEU331 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 668 |
| Details | Domain: {"description":"Tyrosine-protein phosphatase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Motif: {"description":"Glucan phosphatase signature motif CXAGXGR","evidences":[{"source":"PubMed","id":"25544560","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26231210","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Phosphocysteine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11220751","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11739371","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14532330","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22036712","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25538239","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25544560","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25544560","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4RKK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Required for homodimerization","evidences":[{"source":"PubMed","id":"23922729","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
