4PLA
Crystal structure of phosphatidyl inositol 4-kinase II alpha in complex with ATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003796 | molecular_function | lysozyme activity |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004430 | molecular_function | 1-phosphatidylinositol 4-kinase activity |
| A | 0009253 | biological_process | peptidoglycan catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016998 | biological_process | cell wall macromolecule catabolic process |
| A | 0030430 | cellular_component | host cell cytoplasm |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0044659 | biological_process | viral release from host cell by cytolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue ATP A 1201 |
| Chain | Residue |
| A | TRP359 |
| A | ARG360 |
| A | PRO363 |
| A | PHE364 |
| A | ALA367 |
| A | TRP368 |
| A | VAL444 |
| A | GLN445 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue ATP A 1202 |
| Chain | Residue |
| A | GLY133 |
| A | SER134 |
| A | SER137 |
| A | VAL150 |
| A | LYS152 |
| A | GLN261 |
| A | LEU262 |
| A | PHE263 |
| A | VAL264 |
| A | ILE345 |
| A | ASP346 |
| A | HOH1301 |
| A | GLN132 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Region: {"description":"G-loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Region: {"description":"Important for substrate binding","evidences":[{"source":"PubMed","id":"24675427","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 17 |
| Details | Region: {"description":"Important for interaction with membranes","evidences":[{"source":"PubMed","id":"24675427","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Region: {"description":"Catalytic loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | Region: {"description":"Activation loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24675427","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25168678","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"22535966","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24675427","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
