1D2A
CRYSTAL STRUCTURE OF A YEAST LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE (LTP1) COMPLEXED WITH THE ACTIVATOR ADENINE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003993 | molecular_function | acid phosphatase activity |
| A | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| A | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006470 | biological_process | protein dephosphorylation |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0003993 | molecular_function | acid phosphatase activity |
| B | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| B | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006470 | biological_process | protein dephosphorylation |
| B | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 402 |
| Chain | Residue |
| A | ALA13 |
| A | LEU14 |
| A | GLY15 |
| A | ASN16 |
| A | PHE17 |
| A | CYS18 |
| A | ARG19 |
| A | SER20 |
| A | HOH536 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 403 |
| Chain | Residue |
| B | ALA13 |
| B | LEU14 |
| B | GLY15 |
| B | ASN16 |
| B | PHE17 |
| B | CYS18 |
| B | ARG19 |
| B | SER20 |
| B | HOH458 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 404 |
| Chain | Residue |
| A | THR48 |
| A | ASN97 |
| A | ASN100 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ADE B 401 |
| Chain | Residue |
| B | TYR51 |
| B | HIS52 |
| B | ASP132 |
| B | TRP134 |
| B | HOH410 |
| B | HOH458 |
| B | HOH485 |
| B | HOH518 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10684639","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D1Q","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"10684639","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D1Q","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"10684639","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D1Q","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"10684639","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D1Q","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
