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 | 0004693 | molecular_function | cyclin-dependent protein serine/threonine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051301 | biological_process | cell division |
| A | 0051726 | biological_process | regulation of cell cycle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 312 |
| Chain | Residue |
| A | GLN148 |
| A | ASN149 |
| A | ASP162 |
| A | ADP314 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 313 |
| Chain | Residue |
| A | ADP314 |
| A | HOH365 |
| A | HOH366 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADP A 314 |
| Chain | Residue |
| A | GLY32 |
| A | THR33 |
| A | VAL37 |
| A | ALA49 |
| A | LYS51 |
| A | PHE98 |
| A | GLU99 |
| A | MET101 |
| A | ASP104 |
| A | GLN148 |
| A | ASN149 |
| A | LEU151 |
| A | ASP162 |
| A | MG312 |
| A | MG313 |
| A | HOH320 |
| A | HOH333 |
| A | HOH365 |
| A | HOH366 |
| A | GLY30 |
| A | GLU31 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 23 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGEGTYGVVYkAkdsqgri...........VALK |
| Chain | Residue | Details |
| A | VAL29-LYS51 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHrDLKpqNLLI |
| Chain | Residue | Details |
| A | ILE140-ILE152 | |
