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 |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004674 | molecular_function | protein serine/threonine kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue B4Y A 900 |
| Chain | Residue |
| A | ILE82 |
| A | PHE120 |
| A | MET153 |
| A | TYR155 |
| A | MET156 |
| A | ALA215 |
| A | GLY218 |
| A | GLY85 |
| A | ALA86 |
| A | PHE87 |
| A | VAL90 |
| A | ALA103 |
| A | LYS105 |
| A | LEU107 |
| A | ASP117 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue B4Y B 900 |
| Chain | Residue |
| B | ILE82 |
| B | GLY85 |
| B | ALA86 |
| B | PHE87 |
| B | VAL90 |
| B | ALA103 |
| B | LYS105 |
| B | LEU107 |
| B | ASP117 |
| B | PHE120 |
| B | MET153 |
| B | TYR155 |
| B | MET156 |
| B | ALA215 |
| B | ASP216 |
| B | GLY218 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue B4Y C 900 |
| Chain | Residue |
| C | ILE82 |
| C | GLY85 |
| C | ALA86 |
| C | PHE87 |
| C | VAL90 |
| C | ALA103 |
| C | LYS105 |
| C | LEU107 |
| C | ASP117 |
| C | PHE120 |
| C | MET153 |
| C | TYR155 |
| C | MET156 |
| C | ALA215 |
| C | ASP216 |
| C | GLY218 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | binding site for residue B4Y D 900 |
| Chain | Residue |
| D | ILE82 |
| D | GLY85 |
| D | ALA86 |
| D | PHE87 |
| D | VAL90 |
| D | ALA103 |
| D | LYS105 |
| D | LEU107 |
| D | ASP117 |
| D | PHE120 |
| D | MET153 |
| D | TYR155 |
| D | MET156 |
| D | ALA215 |
| D | ASP216 |
| D | GLY218 |
| D | HOH1003 |
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 | |
| C | ASP198 | |
| D | ASP198 | |
| Chain | Residue | Details |
| A | ILE82 | |
| A | LYS105 | |
| B | ILE82 | |
| B | LYS105 | |
| C | ILE82 | |
| C | LYS105 | |
| D | ILE82 | |
| D | LYS105 | |
