6O6Q
Crystal structure of Cka1p, a casein kinase 2 alpha ortholog from Candida albicans
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 | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005829 | cellular_component | cytosol |
A | 0005956 | cellular_component | protein kinase CK2 complex |
A | 0006356 | biological_process | regulation of transcription by RNA polymerase I |
A | 0006359 | biological_process | regulation of transcription by RNA polymerase III |
A | 0006468 | biological_process | protein phosphorylation |
A | 0006974 | biological_process | DNA damage response |
A | 0042273 | biological_process | ribosomal large subunit biogenesis |
A | 0051726 | biological_process | regulation of cell cycle |
A | 0106310 | molecular_function | protein serine kinase activity |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005634 | cellular_component | nucleus |
B | 0005829 | cellular_component | cytosol |
B | 0005956 | cellular_component | protein kinase CK2 complex |
B | 0006356 | biological_process | regulation of transcription by RNA polymerase I |
B | 0006359 | biological_process | regulation of transcription by RNA polymerase III |
B | 0006468 | biological_process | protein phosphorylation |
B | 0006974 | biological_process | DNA damage response |
B | 0042273 | biological_process | ribosomal large subunit biogenesis |
B | 0051726 | biological_process | regulation of cell cycle |
B | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue AMP A 401 |
Chain | Residue |
A | LEU49 |
A | ILE178 |
A | ASP179 |
A | HOH589 |
A | ARG51 |
A | GLY52 |
A | VAL57 |
A | ILE99 |
A | GLU118 |
A | ILE120 |
A | HIS164 |
A | MET167 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 402 |
Chain | Residue |
A | SER297 |
A | GLN298 |
B | ARG306 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 403 |
Chain | Residue |
A | LYS81 |
A | ARG84 |
A | ARG159 |
A | ASN193 |
A | HOH517 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue CL A 404 |
Chain | Residue |
A | PRO24 |
A | GLN25 |
A | SER26 |
B | HOH538 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue CL A 405 |
Chain | Residue |
A | TYR16 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue CL A 406 |
Chain | Residue |
A | ARG66 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue CL A 407 |
Chain | Residue |
A | ARG282 |
A | GLN283 |
B | LYS319 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue GOL A 408 |
Chain | Residue |
A | ARG195 |
A | SER198 |
A | ARG199 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue GOL A 409 |
Chain | Residue |
A | ARG309 |
A | TYR310 |
A | ASP311 |
A | GLU314 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue AMP B 401 |
Chain | Residue |
B | LEU49 |
B | VAL57 |
B | VAL70 |
B | GLU118 |
B | HIS119 |
B | ILE120 |
B | HIS164 |
B | MET167 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue CL B 402 |
Chain | Residue |
B | PRO24 |
B | GLN25 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue CL B 403 |
Chain | Residue |
B | ARG138 |
B | SER297 |
B | GLU299 |
site_id | AD4 |
Number of Residues | 1 |
Details | binding site for residue CL B 405 |
Chain | Residue |
B | ASN280 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue GOL B 406 |
Chain | Residue |
B | VAL296 |
B | GLN298 |
B | HOH517 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGKYSEVFlGidlekrek..........VVIK |
Chain | Residue | Details |
A | LEU49-LYS72 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKphNVMI |
Chain | Residue | Details |
A | ILE156-ILE168 |