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 | 11 |
Details | BINDING SITE FOR RESIDUE 0SW A 501 |
Chain | Residue |
A | ALA50 |
A | LEU158 |
A | ARG356 |
A | ILE79 |
A | PHE97 |
A | ASP98 |
A | TYR99 |
A | ALA100 |
A | ASP103 |
A | HIS106 |
A | ALA155 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 502 |
Chain | Residue |
A | ARG71 |
B | GLN7 |
B | GLN13 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 503 |
Chain | Residue |
A | ARG150 |
A | ASP151 |
A | LEU152 |
A | ILE215 |
A | ASP216 |
A | HOH661 |
A | HOH699 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 504 |
Chain | Residue |
A | ALA177 |
A | ARG178 |
A | LEU179 |
A | PRO186 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 505 |
Chain | Residue |
A | VAL302 |
A | LYS303 |
A | SER306 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 506 |
Chain | Residue |
A | LYS314 |
A | ILE324 |
A | GLN328 |
A | ASP332 |
B | TRP241 |
B | HOH449 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 507 |
Chain | Residue |
A | LYS52 |
A | ASP173 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 301 |
Chain | Residue |
B | ASP-2 |
B | ALA0 |
B | ALA2 |
B | ARG157 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 302 |
Chain | Residue |
B | PHE5 |
B | PRO194 |
B | PHE195 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 303 |
Chain | Residue |
B | GLN49 |
B | GLN59 |
B | ALA63 |
B | TYR156 |
B | TYR184 |
B | ARG185 |
B | HOH430 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 304 |
Chain | Residue |
B | ILE42 |
B | ASN46 |
B | ARG185 |
B | GLU246 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 305 |
Chain | Residue |
B | GLN49 |
B | GLU53 |
B | LEU57 |
B | GLN59 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 306 |
Chain | Residue |
A | LYS83 |
A | VAL84 |
B | ASP147 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 307 |
Chain | Residue |
B | ARG58 |
B | GLN59 |
B | GLN60 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT B 308 |
Chain | Residue |
B | GLN41 |
B | THR45 |
B | THR66 |
B | PHE69 |
B | LYS70 |
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 |
B | SER275 | |
Chain | Residue | Details |
A | VAL27 | |
A | LYS52 | |