Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | binding site for residue 6U2 A 501 |
Chain | Residue |
A | ILE82 |
A | VAL137 |
A | MET153 |
A | GLU154 |
A | MET156 |
A | LEU205 |
A | ALA215 |
A | ASP216 |
A | GLY218 |
A | PHE368 |
A | PHE87 |
A | GLY88 |
A | GLU89 |
A | VAL90 |
A | ALA103 |
A | LYS105 |
A | LEU107 |
A | PHE120 |
site_id | AC2 |
Number of Residues | 20 |
Details | binding site for residue 6U2 B 501 |
Chain | Residue |
B | ILE82 |
B | GLY85 |
B | PHE87 |
B | GLY88 |
B | GLU89 |
B | VAL90 |
B | ALA103 |
B | LYS105 |
B | LEU107 |
B | ASP117 |
B | PHE120 |
B | VAL137 |
B | MET153 |
B | GLU154 |
B | TYR155 |
B | MET156 |
B | LEU205 |
B | ASP216 |
B | GLY218 |
B | PHE368 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGAFGEVQlVrhkstrkv..........YAMK |
Chain | Residue | Details |
A | ILE82-LYS105 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. FiHrDVKpdNMLL |
Chain | Residue | Details |
A | PHE194-LEU206 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP198 | |
B | ASP198 | |
Chain | Residue | Details |
A | ILE82 | |
A | LYS105 | |
B | ILE82 | |
B | LYS105 | |