7A22
Crystal structure of human protein kinase CK2alpha' (CSNK2A2 gene product) in complex with the ATP-competitive inhibitor 5,6,7-tribromo-1H-triazolo[4,5-b]pyridine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0006468 | biological_process | protein phosphorylation |
| A | 0006915 | biological_process | apoptotic process |
| A | 0006974 | biological_process | DNA damage response |
| A | 0007283 | biological_process | spermatogenesis |
| A | 0016055 | biological_process | Wnt signaling pathway |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0021987 | biological_process | cerebral cortex development |
| A | 0031507 | biological_process | heterochromatin formation |
| A | 0031519 | cellular_component | PcG protein complex |
| A | 0032435 | biological_process | negative regulation of proteasomal ubiquitin-dependent protein catabolic process |
| A | 0035102 | cellular_component | PRC1 complex |
| A | 0042176 | biological_process | regulation of protein catabolic process |
| A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| 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 | 7 |
| Details | binding site for residue EDO A 401 |
| Chain | Residue |
| A | ARG279 |
| A | LYS280 |
| A | ARG281 |
| A | TRP282 |
| A | GLU283 |
| A | ASP303 |
| A | HOH688 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue QWW A 402 |
| Chain | Residue |
| A | ILE96 |
| A | PHE114 |
| A | GLU115 |
| A | ILE117 |
| A | MET164 |
| A | ILE175 |
| A | EDO403 |
| A | HOH505 |
| A | VAL54 |
| A | VAL67 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | LYS69 |
| A | PHE114 |
| A | ASP176 |
| A | QWW402 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | VAL12 |
| A | HIS149 |
| A | TYR212 |
| A | MET216 |
| A | ALA316 |
| A | HOH564 |
| A | HOH573 |
| A | HOH599 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | PHE122 |
| A | LYS123 |
| A | PRO160 |
| A | PHE198 |
| A | GLU231 |
| A | EDO413 |
| A | HOH660 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | LEU42 |
| A | ILE70 |
| A | GLU318 |
| A | GLU321 |
| A | HIS322 |
| A | HOH524 |
| A | HOH576 |
| A | HOH724 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | ASP133 |
| A | PHE136 |
| A | TYR137 |
| A | HIS167 |
| A | LYS170 |
| A | HOH514 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 408 |
| Chain | Residue |
| A | LEU86 |
| A | LEU89 |
| A | ARG90 |
| A | GLY91 |
| A | ILE96 |
| A | LYS97 |
| A | LEU98 |
| A | HOH606 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 409 |
| Chain | Residue |
| A | TYR13 |
| A | ALA14 |
| A | GLU15 |
| A | VAL16 |
| A | HOH651 |
| site_id | AD1 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 410 |
| Chain | Residue |
| A | ASN94 |
| A | GLU140 |
| A | LYS170 |
| A | LYS171 |
| A | LEU172 |
| A | ARG173 |
| A | LYS260 |
| A | HOH682 |
| A | HOH738 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 411 |
| Chain | Residue |
| A | ARG81 |
| A | ARG156 |
| A | LEU179 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 412 |
| Chain | Residue |
| A | SER18 |
| A | ARG245 |
| A | HOH554 |
| A | HOH692 |
| A | HOH752 |
| A | HOH788 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 413 |
| Chain | Residue |
| A | LYS123 |
| A | HIS235 |
| A | EDO405 |
| A | HOH507 |
| A | HOH526 |
| A | HOH676 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 414 |
| Chain | Residue |
| A | ARG192 |
| A | VAL193 |
| A | ALA194 |
| A | LYS199 |
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 | 285 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
