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Ligands
Code Name Style Show Link
RFZ 5,6-dichloro-1-beta-D-ribofuranosyl-1h-benzimidazole
CL Chloride ion
Non-standard Residues
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Glycosylation
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Modification
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Code : 3H30   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Crystal structure of the catalytic subunit of human protein kinase CK2 with 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole
Release Data : 2009-05-12
Compound :
mol_id molecule chains synonym
1 Casein kinase II subunit alpha A,B CK II
ec: 2.7.11.1
fragment: catalytic subunit, residues 1-334
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: CSNK2A1, CK2A1
expression_system_strain: BL21(DE3)
expression_system_vector_type: Plasmid
expression_system_plasmid: PT7-7
Authors : Niefind, K., Raaf, J., Issinger, O.-G.
Keywords : Protein kinase CK2, Casein kinase 2, Casein kinase II, ATP-binding, Kinase, Nucleotide-binding, Phosphoprotein, Serine/threonine-protein kinase, Transferase, Wnt signaling pathway
Exp. method : X-RAY DIFFRACTION ( 1.56 Å )
Citation :

The CK2alpha/CK2beta Interface of Human Protein Kinase CK2 Harbors a Binding Pocket for Small Molecules

Raaf, J.,Brunstein, E.,Issinger, O.-G.  et al.
(2008)  Chem.Biol.  15 : 111 - 117

PubMed: 18291315
DOI: 10.1016/j.chembiol.2007.12.012

Evolved to be active: sulfate ions define substrate recognition sites of CK2alpha and emphasise its exceptional role within the CMGC family of eukaryotic protein kinases

Niefind, K.,Yde, C.W.,Ermakova, I.  et al.
(2007)  J.Mol.Biol.  370 : 427 - 438

PubMed: 17524418
DOI: 10.1016/j.jmb.2007.04.068

Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit

Ermakova, I.,Boldyreff, B.,Issinger, O.-G.  et al.
(2003)  J.Mol.Biol.  330 : 925 - 934

PubMed: 12860116

Chain : A, B
UniProt : P68400 (CSK21_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein] 2.7.11.1 PubMed:20545769, PubMed:20625391, PubMed:21482717, PubMed:22184066, PubMed:23123191, PubMed:30699359, PubMed:30898438, PubMed:31439799
left-to-right PubMed:20545769, PubMed:21482717, PubMed:23123191, PubMed:30699359, PubMed:30898438, PubMed:31439799, PubMed:35597237
ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein] 2.7.11.1 PubMed:20625391, PubMed:22325354, PubMed:31439799
left-to-right PubMed:31439799