1DJY
PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH INOSITOL-2,4,5-TRISPHOSPHATE
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 PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 2 |
| Chain | Residue |
| A | I2P1 |
| A | ASN312 |
| A | GLU341 |
| A | ASP343 |
| A | GLU390 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 3 |
| Chain | Residue |
| A | ILE651 |
| A | ASP653 |
| A | ASN677 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 4 |
| Chain | Residue |
| A | ASP706 |
| A | TYR707 |
| A | ASP653 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 5 |
| Chain | Residue |
| A | GLY583 |
| A | PRO584 |
| A | ASP587 |
| A | ARG701 |
| A | PHE715 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 2 |
| Chain | Residue |
| B | I2P1 |
| B | ASN312 |
| B | GLU341 |
| B | ASP343 |
| B | GLU390 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA B 3 |
| Chain | Residue |
| B | ILE651 |
| B | ASP653 |
| B | ASN677 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 4 |
| Chain | Residue |
| B | ASP653 |
| B | ASP706 |
| B | TYR707 |
| B | ASP708 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 5 |
| Chain | Residue |
| B | GLY583 |
| B | PRO584 |
| B | ASP587 |
| B | ARG701 |
| B | PHE715 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE I2P A 1 |
| Chain | Residue |
| A | CA2 |
| A | HIS311 |
| A | ASN312 |
| A | GLU341 |
| A | ASP343 |
| A | HIS356 |
| A | GLU390 |
| A | LYS438 |
| A | SER522 |
| A | ARG549 |
| A | TYR551 |
| A | HOH923 |
| site_id | BC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE I2P B 1 |
| Chain | Residue |
| B | CA2 |
| B | HIS311 |
| B | ASN312 |
| B | GLU341 |
| B | ASP343 |
| B | HIS356 |
| B | SER388 |
| B | GLU390 |
| B | LYS438 |
| B | SER522 |
| B | ARG549 |
| B | TYR551 |
| B | HOH900 |
| B | HOH901 |
| B | HOH937 |
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 |
| B | HIS311 | |
| B | HIS356 | |
| A | HIS311 | |
| A | HIS356 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 |
| Chain | Residue | Details |
| A | ASP157 | |
| A | LYS159 | |
| A | GLU164 | |
| B | ASP153 | |
| B | ASN155 | |
| B | ASP157 | |
| B | LYS159 | |
| B | GLU164 | |
| B | ASP189 | |
| B | SER191 | |
| B | THR193 | |
| B | SER195 | |
| B | GLU200 | |
| A | ASP153 | |
| A | ASN155 | |
| A | ASP189 | |
| A | SER191 | |
| A | THR193 | |
| A | SER195 | |
| A | GLU200 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN677 | |
| A | ASP706 | |
| A | TYR707 | |
| A | ASP708 | |
| B | ASN312 | |
| B | GLU341 | |
| B | ASP343 | |
| B | GLU390 | |
| B | LYS438 | |
| B | LYS440 | |
| B | SER522 | |
| B | ARG549 | |
| B | ILE651 | |
| B | ASP653 | |
| B | ASN677 | |
| B | ASP706 | |
| B | TYR707 | |
| B | ASP708 | |
| A | ASN312 | |
| A | GLU341 | |
| A | ASP343 | |
| A | GLU390 | |
| A | LYS438 | |
| A | LYS440 | |
| A | SER522 | |
| A | ARG549 | |
| A | ILE651 | |
| A | ASP653 |
| 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 | 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 |
