3S3H
Crystal structure of the catalytic domain of PTP10D from Drosophila melanogaster with a phosphopeptide substrate GP4
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 | 1 |
| Details | BINDING SITE FOR RESIDUE 1BO A 308 |
| Chain | Residue |
| A | LEU80 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BU1 A 309 |
| Chain | Residue |
| B | TYR267 |
Functional Information from PROSITE/UniProt
| site_id | PS00383 |
| Number of Residues | 11 |
| Details | TYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGvgRSG |
| Chain | Residue | Details |
| A | VAL240-GLY250 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 510 |
| 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 | 2 |
| Details | Active site: {"description":"Phosphocysteine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10044","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
