1QAS
1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA 1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004435 | molecular_function | phosphatidylinositol 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 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 | 4 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | HIS311 | |
A | HIS356 | |
B | HIS311 | |
B | HIS356 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 |
Chain | Residue | Details |
A | ASP153 | |
A | GLU200 | |
B | ASP153 | |
B | ASN155 | |
B | ASP157 | |
B | LYS159 | |
B | GLU164 | |
B | ASP189 | |
B | SER191 | |
B | THR193 | |
B | SER195 | |
A | ASN155 | |
B | GLU200 | |
A | ASP157 | |
A | LYS159 | |
A | GLU164 | |
A | ASP189 | |
A | SER191 | |
A | THR193 | |
A | SER195 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | BINDING: |
Chain | Residue | Details |
A | ASN312 | |
A | ASP653 | |
A | ASN677 | |
A | ASP706 | |
A | TYR707 | |
A | ASP708 | |
B | ASN312 | |
B | GLU341 | |
B | ASP343 | |
B | GLU390 | |
B | LYS438 | |
A | GLU341 | |
B | LYS440 | |
B | SER522 | |
B | ARG549 | |
B | ILE651 | |
B | ASP653 | |
B | ASN677 | |
B | ASP706 | |
B | TYR707 | |
B | ASP708 | |
A | ASP343 | |
A | GLU390 | |
A | LYS438 | |
A | LYS440 | |
A | SER522 | |
A | ARG549 | |
A | ILE651 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q8R3B1 |
Chain | Residue | Details |
A | THR457 | |
B | THR457 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P51178 |
Chain | Residue | Details |
A | SER460 | |
B | SER460 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | CARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:24098488 |
Chain | Residue | Details |
A | SER191 | |
B | SER191 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | CARBOHYD: O-linked (GlcNAc) threonine => ECO:0000269|PubMed:24098488 |
Chain | Residue | Details |
A | THR193 | |
B | THR193 |
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 |