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 | 14 |
| Details | binding site for residue 3SG A 501 |
| Chain | Residue |
| A | ILE98 |
| A | MET172 |
| A | ASP218 |
| A | ASN219 |
| A | ASP232 |
| A | PHE384 |
| A | ALA102 |
| A | PHE103 |
| A | VAL106 |
| A | ALA119 |
| A | PHE136 |
| A | MET169 |
| A | GLU170 |
| A | TYR171 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue 3SG B 501 |
| Chain | Residue |
| B | ILE98 |
| B | GLY101 |
| B | ALA102 |
| B | PHE103 |
| B | GLY104 |
| B | VAL106 |
| B | ALA119 |
| B | PHE136 |
| B | MET169 |
| B | GLU170 |
| B | MET172 |
| B | ASP214 |
| B | ASN219 |
| B | ASP232 |
| B | THR235 |
| B | PHE384 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue 3SG C 501 |
| Chain | Residue |
| C | GLY101 |
| C | ALA102 |
| C | PHE103 |
| C | GLY104 |
| C | ALA119 |
| C | PHE136 |
| C | GLU170 |
| C | MET172 |
| C | ASP214 |
| C | ASP218 |
| C | ASN219 |
| C | ALA231 |
| C | ASP232 |
| C | PHE384 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue 3SG D 501 |
| Chain | Residue |
| D | ILE98 |
| D | ALA102 |
| D | PHE103 |
| D | VAL106 |
| D | ALA119 |
| D | PHE136 |
| D | MET169 |
| D | GLU170 |
| D | MET172 |
| D | ASP218 |
| D | ASN219 |
| D | ASP232 |
| D | VAL251 |
| D | PHE384 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGAFGEVQlVrhkasqkv..........YAMK |
| Chain | Residue | Details |
| A | ILE98-LYS121 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiHrDVKpdNMLL |
| Chain | Residue | Details |
| A | LEU210-LEU222 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ASP214 | |
| B | ASP214 | |
| C | ASP214 | |
| D | ASP214 | |
| Chain | Residue | Details |
| A | ILE98 | |
| A | LYS121 | |
| B | ILE98 | |
| B | LYS121 | |
| C | ILE98 | |
| C | LYS121 | |
| D | ILE98 | |
| D | LYS121 | |
| Chain | Residue | Details |
| A | THR414 | |
| B | THR414 | |
| C | THR414 | |
| D | THR414 | |
