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 | 16 |
Details | BINDING SITE FOR RESIDUE 0SS A 501 |
Chain | Residue |
A | VAL27 |
A | ASP173 |
A | MET174 |
A | ARG356 |
A | HOH603 |
A | HOH614 |
A | HOH633 |
A | HOH649 |
A | TYR32 |
A | SER62 |
A | GLU66 |
A | ILE79 |
A | PHE97 |
A | TRP105 |
A | HIS149 |
A | ALA172 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE DMS A 502 |
Chain | Residue |
A | LYS153 |
A | HOH608 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO A 503 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO A 504 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 505 |
Chain | Residue |
A | PRO124 |
A | GLY126 |
A | MET127 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 506 |
Chain | Residue |
A | ARG13 |
A | GLU14 |
A | VAL84 |
A | PHE85 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT A 507 |
Chain | Residue |
A | VAL84 |
B | ASP147 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT A 508 |
Chain | Residue |
A | GLU21 |
A | TYR22 |
A | GLU23 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 301 |
Chain | Residue |
B | ALA0 |
B | ALA2 |
B | VAL152 |
B | TYR153 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 302 |
Chain | Residue |
B | GLN49 |
B | GLU53 |
B | LEU57 |
B | GLN59 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO B 303 |
Chain | Residue |
B | GLN161 |
B | TYR162 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 304 |
Chain | Residue |
A | LEU9 |
B | TYR76 |
B | TYR141 |
B | GLU144 |
B | LEU145 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 305 |
Chain | Residue |
A | THR57 |
A | ILE59 |
B | PHE92 |
B | LYS96 |
B | HOH422 |
B | HOH438 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT B 306 |
Chain | Residue |
B | ASN46 |
B | ARG185 |
B | GLU246 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT B 307 |
Chain | Residue |
B | GLN41 |
B | THR45 |
B | THR66 |
B | PHE69 |
B | LYS70 |
B | TYR184 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT B 308 |
Chain | Residue |
B | THR118 |
B | ARG119 |
B | PHE120 |
B | SER121 |
B | ARG247 |
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 | LYS52 | |
A | VAL27 | |