1DJG
PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH LANTHANUM
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 PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 5 |
| Chain | Residue |
| A | GLY583 |
| A | PRO584 |
| A | ASP587 |
| A | ARG701 |
| A | PHE715 |
| A | LYS738 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 5 |
| Chain | Residue |
| B | PHE715 |
| B | HOH957 |
| B | PRO584 |
| B | ASP587 |
| B | ARG701 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LA A 1 |
| Chain | Residue |
| A | ASN312 |
| A | ASP343 |
| A | GLU390 |
| A | HOH1018 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE LA A 2 |
| Chain | Residue |
| A | SER650 |
| A | ILE651 |
| A | ASP653 |
| A | ASN677 |
| A | HOH932 |
| A | HOH1032 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE LA A 3 |
| Chain | Residue |
| A | ASP653 |
| A | ASP706 |
| A | TYR707 |
| A | ASP708 |
| A | HOH1053 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LA A 4 |
| Chain | Residue |
| A | ASP706 |
| A | ASP708 |
| A | ASP714 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LA B 1 |
| Chain | Residue |
| B | ASN312 |
| B | ASP343 |
| B | GLU390 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE LA B 2 |
| Chain | Residue |
| B | ILE651 |
| B | ASP653 |
| B | ASN677 |
| B | HOH918 |
| B | HOH920 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE LA B 3 |
| Chain | Residue |
| B | LA4 |
| B | ASP653 |
| B | ASP706 |
| B | TYR707 |
| B | ASP708 |
| B | HOH1048 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LA B 4 |
| Chain | Residue |
| B | LA3 |
| B | ASP706 |
| B | ASP708 |
| B | ASP714 |
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 | 234 |
| 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 | 256 |
| Details | Domain: {"description":"C2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00041","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 28 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 35 |
| Details | Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"PubMed","id":"24098488","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (GlcNAc) threonine","evidences":[{"source":"PubMed","id":"24098488","evidenceCode":"ECO:0000269"}]} |
| 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 |
