Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0000307 | cellular_component | cyclin-dependent protein kinase holoenzyme complex |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
B | 0016538 | molecular_function | cyclin-dependent protein serine/threonine kinase regulator activity |
B | 0016592 | cellular_component | mediator complex |
B | 0042802 | molecular_function | identical protein binding |
B | 0045023 | biological_process | G0 to G1 transition |
B | 0045746 | biological_process | negative regulation of Notch signaling pathway |
B | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
B | 1990508 | cellular_component | CKM complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue 6A7 A 401 |
Chain | Residue |
A | VAL27 |
A | ALA100 |
A | ALA155 |
A | LEU158 |
A | ASP173 |
A | ARG356 |
A | GLY28 |
A | TYR32 |
A | ALA50 |
A | LYS52 |
A | ILE79 |
A | PHE97 |
A | ASP98 |
A | TYR99 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue EDO A 402 |
Chain | Residue |
A | ARG125 |
A | VAL302 |
A | LYS303 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue FMT A 403 |
Chain | Residue |
A | HIS149 |
A | ASP151 |
A | ASP173 |
A | PHE176 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue FMT A 404 |
Chain | Residue |
A | TYR32 |
A | LYS52 |
A | SER62 |
A | ALA63 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue FMT A 405 |
Chain | Residue |
A | GLU17 |
A | TYR22 |
A | SER87 |
A | ASP90 |
A | TRP94 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue FMT B 301 |
Chain | Residue |
B | ALA2 |
B | GLY3 |
B | TYR153 |
B | ARG157 |
B | FMT302 |
B | HOH414 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue FMT B 302 |
Chain | Residue |
B | ALA0 |
B | TYR153 |
B | FMT301 |
B | HOH437 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue FMT B 303 |
Chain | Residue |
B | HIS203 |
B | LYS211 |
B | ASP212 |
B | ALA213 |
B | ARG214 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 26 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGRGTYGHVYkAkrkdgkddkd........YALK |
Chain | Residue | Details |
A | VAL27-LYS52 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpaNILV |
Chain | Residue | Details |
A | VAL147-VAL159 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP151 | |
Chain | Residue | Details |
A | VAL27 | |
A | LYS52 | |