4WTV
Crystal structure of the phosphatidylinositol 4-kinase IIbeta
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003796 | molecular_function | lysozyme activity |
A | 0004430 | molecular_function | 1-phosphatidylinositol 4-kinase activity |
A | 0009253 | biological_process | peptidoglycan catabolic process |
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 |
B | 0003796 | molecular_function | lysozyme activity |
B | 0004430 | molecular_function | 1-phosphatidylinositol 4-kinase activity |
B | 0009253 | biological_process | peptidoglycan catabolic process |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0016998 | biological_process | cell wall macromolecule catabolic process |
B | 0030430 | cellular_component | host cell cytoplasm |
B | 0031640 | biological_process | killing of cells of another organism |
B | 0042742 | biological_process | defense response to bacterium |
B | 0044659 | biological_process | viral release from host cell by cytolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | binding site for residue ATP A 1201 |
Chain | Residue |
A | SER133 |
A | HOH1322 |
A | HOH1367 |
A | HOH1426 |
A | HOH1433 |
B | TYR268 |
B | ARG271 |
B | LYS272 |
A | VAL146 |
A | LYS148 |
A | GLN257 |
A | LEU258 |
A | PHE259 |
A | VAL260 |
A | ILE343 |
A | ASP344 |
site_id | AC2 |
Number of Residues | 18 |
Details | binding site for residue ATP B 1201 |
Chain | Residue |
A | ARG271 |
A | LYS272 |
B | SER131 |
B | SER133 |
B | PHE135 |
B | VAL146 |
B | LYS148 |
B | GLN257 |
B | LEU258 |
B | PHE259 |
B | VAL260 |
B | ILE343 |
B | ASP344 |
B | HOH1349 |
B | HOH1360 |
B | HOH1399 |
B | HOH1436 |
B | HOH1446 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26143926, ECO:0007744|PDB:4WTV |
Chain | Residue | Details |
A | SER133 | |
B | ASP344 | |
A | LYS148 | |
A | GLN257 | |
A | ARG271 | |
A | ASP344 | |
B | SER133 | |
B | LYS148 | |
B | GLN257 | |
B | ARG271 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | GLU1010 | |
B | GLU1010 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | ASP1019 | |
B | ASP1019 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | LEU1031 | |
A | PHE1103 | |
B | LEU1031 | |
B | PHE1103 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
Chain | Residue | Details |
A | SER1116 | |
A | ASN1131 | |
B | SER1116 | |
B | ASN1131 |