7A1Z
Crystal structure of human protein kinase CK2alpha' (CSNK2A2 gene product) in complex with the ATP-competitive inhibitor 6-bromo-5-chloro-1H-triazolo[4,5-b]pyridine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000785 | cellular_component | chromatin |
A | 0001669 | cellular_component | acrosomal vesicle |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005956 | cellular_component | protein kinase CK2 complex |
A | 0006302 | biological_process | double-strand break repair |
A | 0006338 | biological_process | chromatin remodeling |
A | 0006468 | biological_process | protein phosphorylation |
A | 0006915 | biological_process | apoptotic process |
A | 0007283 | biological_process | spermatogenesis |
A | 0016055 | biological_process | Wnt signaling pathway |
A | 0016310 | biological_process | phosphorylation |
A | 0021987 | biological_process | cerebral cortex development |
A | 0031519 | cellular_component | PcG protein complex |
A | 0032435 | biological_process | negative regulation of proteasomal ubiquitin-dependent protein catabolic process |
A | 0044024 | molecular_function | histone H2AS1 kinase activity |
A | 0051726 | biological_process | regulation of cell cycle |
A | 0097421 | biological_process | liver regeneration |
A | 0106310 | molecular_function | protein serine kinase activity |
A | 1901524 | biological_process | regulation of mitophagy |
A | 1903955 | biological_process | positive regulation of protein targeting to mitochondrion |
A | 1905818 | biological_process | regulation of chromosome separation |
A | 2001234 | biological_process | negative regulation of apoptotic signaling pathway |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue QWN A 401 |
Chain | Residue |
A | LYS69 |
A | ILE96 |
A | PHE114 |
A | GLU115 |
A | MET164 |
A | ILE175 |
A | ASP176 |
A | HOH540 |
A | HOH607 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue CL A 402 |
Chain | Residue |
A | ARG156 |
A | ASN190 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue EDO A 403 |
Chain | Residue |
A | PHE136 |
A | GLU140 |
A | VAL328 |
A | GLU331 |
A | GLN332 |
A | HOH502 |
A | HOH514 |
A | HOH722 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue EDO A 404 |
Chain | Residue |
A | TYR13 |
A | ALA14 |
A | GLU15 |
A | VAL16 |
A | LEU19 |
A | HOH674 |
A | HOH680 |
A | HOH682 |
A | HOH712 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue EDO A 405 |
Chain | Residue |
A | TRP34 |
A | GLY35 |
A | LYS108 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO A 406 |
Chain | Residue |
A | PHE122 |
A | LYS123 |
A | TYR197 |
A | PHE198 |
A | GLU231 |
A | HOH646 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO A 407 |
Chain | Residue |
A | TYR308 |
A | ASP309 |
A | GLN312 |
A | HOH523 |
A | HOH716 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue EDO A 408 |
Chain | Residue |
A | LEU42 |
A | PHE55 |
A | GLU318 |
A | GLU321 |
A | HIS322 |
A | HOH507 |
A | HOH508 |
A | HOH515 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGKYSEVFeAinitnner..........VVVK |
Chain | Residue | Details |
A | LEU46-LYS69 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKphNVMI |
Chain | Residue | Details |
A | ILE153-ILE165 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
Chain | Residue | Details |
A | ASP157 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | LEU46 | |
A | LYS69 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195 |
Chain | Residue | Details |
A | TYR13 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER18 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195 |
Chain | Residue | Details |
A | SER21 | |
A | SER288 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS97 |