1QAS
1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA 1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004435 | molecular_function | phosphatidylinositol-4,5-bisphosphate phospholipase C activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0007165 | biological_process | signal transduction |
| A | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| A | 0035556 | biological_process | intracellular signal transduction |
| B | 0004435 | molecular_function | phosphatidylinositol-4,5-bisphosphate phospholipase C activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0007165 | biological_process | signal transduction |
| B | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| B | 0035556 | biological_process | intracellular signal transduction |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DKNKDNKMNfkEL |
| Chain | Residue | Details |
| A | ASP153-LEU165 | |
| A | ASP189-ILE201 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 288 |
| Details | Domain: {"description":"PI-PLC X-box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00270","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 117 |
| Details | Domain: {"description":"PI-PLC Y-box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00271","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 28 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 2isd |
| Chain | Residue | Details |
| A | HIS356 | |
| A | HIS311 | |
| A | GLU341 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 2isd |
| Chain | Residue | Details |
| B | HIS356 | |
| B | HIS311 | |
| B | GLU341 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 28 |
| Chain | Residue | Details |
| A | HIS311 | electrostatic stabiliser, hydrogen bond donor |
| A | ASN312 | metal ligand |
| A | GLU341 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, metal ligand |
| A | ASP343 | metal ligand |
| A | HIS356 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU390 | hydrogen bond acceptor, hydrogen bond donor, increase acidity, metal ligand, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 28 |
| Chain | Residue | Details |
| B | HIS311 | electrostatic stabiliser, hydrogen bond donor |
| B | ASN312 | metal ligand |
| B | GLU341 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, metal ligand |
| B | ASP343 | metal ligand |
| B | HIS356 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU390 | hydrogen bond acceptor, hydrogen bond donor, increase acidity, metal ligand, proton acceptor, proton donor |
