Brand  (β version)

PDB ID: 3U9C

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Ligands
Code Name Style Show Link
SO4 Sulfate ion PoSSuM
04G 7-hydroxy-3h-phenoxazin-3-one PoSSuM
GOL Glycerol PoSSuM
CL Chloride ion PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 3U9C   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE/TRANSFERASE INHIBITOR
Title : Structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit with the ATP-competitive inhibitor resorufin
Release Data : 2012-05-30
Compound :
mol_id molecule chains synonym
1 Casein kinase II subunit alpha A,B CK II alpha
ec: 2.7.11.1
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: CSNK2A1, CK2A1
Authors : Klopffleisch, K., Issinger, O.-G., Niefind, K.
Keywords : protein kinase CK2 casein kinase 2, eukaryotic protein kinase fold, ATP:protein phosphotransferase, protein kinase, ATP CK2beta, TRANSFERASE-TRANSFERASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 3.200 Å )
Citation :

Low-density crystal packing of human protein kinase CK2 catalytic subunit in complex with resorufin or other ligands: a tool to study the unique hinge-region plasticity of the enzyme without packing bias.

Klopffleisch, K.,Issinger, O.G.,Niefind, K.
(2012)  Acta Crystallogr.,Sect.D  68 : 883 - 892

PubMed: 22868753
DOI: 10.1107/S0907444912016587

Conformational plasticity of the catalytic subunit of protein kinase CK2 and its consequences for regulation and drug design.

Niefind, K.,Issinger, O.G.
(2010)  Biochim.Biophys.Acta  1804 : 484 - 492

PubMed: 19796713
DOI: 10.1016/j.bbapap.2009.09.022

The CK2 alpha/CK2 beta 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

Protein kinase CK2 in health and disease: Protein kinase CK2: from structures to insights.

Niefind, K.,Raaf, J.,Issinger, O.G.
(2009)  Cell.Mol.Life Sci.  66 : 1800 - 1816

PubMed: 19387553
DOI: 10.1007/s00018-009-9149-8

Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate.

Yde, C.W.,Ermakova, I.,Issinger, O.G.  et al.
(2005)  J.Mol.Biol.  347 : 399 - 414

PubMed: 15740749
DOI: 10.1016/j.jmb.2005.01.003

Reaction

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