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 | 0016310 | biological_process | 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 | 10 |
Details | BINDING SITE FOR RESIDUE IXM A 401 |
Chain | Residue |
A | VAL29 |
A | LEU151 |
A | GLU31 |
A | VAL37 |
A | ALA49 |
A | GLU99 |
A | PHE100 |
A | MET101 |
A | GLU102 |
A | LYS107 |
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 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | GLN148 | |
A | ASP144 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP144 | |
A | LYS146 | |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | THR182 | |
A | ASP144 | |
A | LYS146 | |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASN149 | |
A | ASP144 | |
A | LYS146 | |