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 | 19 |
| Details | BINDING SITE FOR RESIDUE BAX A 465 |
| Chain | Residue |
| A | ALA50 |
| A | TYR99 |
| A | ALA100 |
| A | GLU101 |
| A | LEU142 |
| A | VAL147 |
| A | HIS149 |
| A | ILE171 |
| A | ALA172 |
| A | ASP173 |
| A | PHE176 |
| A | LYS52 |
| A | GLU66 |
| A | LEU70 |
| A | LEU73 |
| A | VAL78 |
| A | ILE79 |
| A | PHE97 |
| A | ASP98 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 466 |
| Chain | Residue |
| A | TRP267 |
| A | MET273 |
| A | ASP319 |
| A | PRO320 |
| A | HOH489 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 467 |
| Chain | Residue |
| A | PRO341 |
| A | THR342 |
| A | SER343 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 468 |
| Chain | Residue |
| A | ARG125 |
| A | LYS303 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 469 |
| Chain | Residue |
| A | HIS75 |
| A | PRO76 |
| A | HOH508 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 284 |
| Chain | Residue |
| B | GLN41 |
| B | THR45 |
| B | THR66 |
| B | PHE69 |
| B | LYS70 |
| B | TYR184 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 285 |
| Chain | Residue |
| A | ASP2 |
| A | PHE5 |
| B | TYR76 |
| B | SER77 |
| B | LYS79 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 286 |
| Chain | Residue |
| B | ASN46 |
| B | ARG185 |
| B | TRP241 |
| B | PHE244 |
| B | GLU246 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 287 |
| Chain | Residue |
| B | GLU53 |
| B | LEU57 |
| B | GLN59 |
| B | ILE62 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 288 |
| Chain | Residue |
| B | GLN13 |
| B | TRP14 |
| B | ARG75 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 289 |
| Chain | Residue |
| B | ASN133 |
| B | HIS134 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 290 |
| Chain | Residue |
| B | ARG25 |
| B | GLU34 |
| B | TYR37 |
| B | TRP38 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 291 |
| Chain | Residue |
| B | ALA0 |
| B | ALA2 |
| B | GLN60 |
| B | VAL152 |
| B | ARG157 |
| B | HOH342 |
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 | |
