Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004693 | molecular_function | cyclin-dependent protein serine/threonine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
A | 0042127 | biological_process | regulation of cell population proliferation |
A | 0043697 | biological_process | cell dedifferentiation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue N1J A 401 |
Chain | Residue |
A | ILE19 |
A | ASP163 |
A | HOH509 |
A | HOH532 |
A | VAL27 |
A | ALA41 |
A | LYS43 |
A | PHE98 |
A | GLU99 |
A | VAL101 |
A | GLN149 |
A | LEU152 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 25 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGAYGKVFkArdlknggrf.........VALK |
Chain | Residue | Details |
A | ILE19-LYS43 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpqNILV |
Chain | Residue | Details |
A | VAL141-VAL153 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | ASP145 | |
Chain | Residue | Details |
A | ILE19 | |
A | LYS43 | |
Chain | Residue | Details |
A | TYR13 | |
Chain | Residue | Details |
A | TYR24 | |
Chain | Residue | Details |
A | THR49 | |
A | THR70 | |
Chain | Residue | Details |
A | THR177 | |
Chain | Residue | Details |
A | LYS264 | |