Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4NH1

Crystal structure of a heterotetrameric CK2 holoenzyme complex carrying the Andante-mutation in CK2beta and consistent with proposed models of autoinhibition and trans-autophosphorylation

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	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0000785	cellular_component	chromatin
C	0001650	cellular_component	fibrillar center
C	0003682	molecular_function	chromatin binding
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0005102	molecular_function	signaling receptor binding
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0005956	cellular_component	protein kinase CK2 complex
C	0007165	biological_process	signal transduction
C	0008285	biological_process	negative regulation of cell population proliferation
C	0016055	biological_process	Wnt signaling pathway
C	0016605	cellular_component	PML body
C	0019887	molecular_function	protein kinase regulator activity
C	0019904	molecular_function	protein domain specific binding
C	0030674	molecular_function	protein-macromolecule adaptor activity
C	0031507	biological_process	heterochromatin formation
C	0031519	cellular_component	PcG protein complex
C	0032435	biological_process	negative regulation of proteasomal ubiquitin-dependent protein catabolic process
C	0032927	biological_process	positive regulation of activin receptor signaling pathway
C	0033211	biological_process	adiponectin-activated signaling pathway
C	0034774	cellular_component	secretory granule lumen
C	0042802	molecular_function	identical protein binding
C	0043537	biological_process	negative regulation of blood vessel endothelial cell migration
C	0045893	biological_process	positive regulation of DNA-templated transcription
C	0046872	molecular_function	metal ion binding
C	0060391	biological_process	positive regulation of SMAD protein signal transduction
C	0061154	biological_process	endothelial tube morphogenesis
C	0061629	molecular_function	RNA polymerase II-specific DNA-binding transcription factor binding
C	0065003	biological_process	protein-containing complex assembly
C	0070062	cellular_component	extracellular exosome
C	0075342	biological_process	symbiont-mediated disruption of host cell PML body
C	1903901	biological_process	negative regulation of viral life cycle
C	1904813	cellular_component	ficolin-1-rich granule lumen
D	0000785	cellular_component	chromatin
D	0001650	cellular_component	fibrillar center
D	0003682	molecular_function	chromatin binding
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0005102	molecular_function	signaling receptor binding
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0005956	cellular_component	protein kinase CK2 complex
D	0007165	biological_process	signal transduction
D	0008285	biological_process	negative regulation of cell population proliferation
D	0016055	biological_process	Wnt signaling pathway
D	0016605	cellular_component	PML body
D	0019887	molecular_function	protein kinase regulator activity
D	0019904	molecular_function	protein domain specific binding
D	0030674	molecular_function	protein-macromolecule adaptor activity
D	0031507	biological_process	heterochromatin formation
D	0031519	cellular_component	PcG protein complex
D	0032435	biological_process	negative regulation of proteasomal ubiquitin-dependent protein catabolic process
D	0032927	biological_process	positive regulation of activin receptor signaling pathway
D	0033211	biological_process	adiponectin-activated signaling pathway
D	0034774	cellular_component	secretory granule lumen
D	0042802	molecular_function	identical protein binding
D	0043537	biological_process	negative regulation of blood vessel endothelial cell migration
D	0045893	biological_process	positive regulation of DNA-templated transcription
D	0046872	molecular_function	metal ion binding
D	0060391	biological_process	positive regulation of SMAD protein signal transduction
D	0061154	biological_process	endothelial tube morphogenesis
D	0061629	molecular_function	RNA polymerase II-specific DNA-binding transcription factor binding
D	0065003	biological_process	protein-containing complex assembly
D	0070062	cellular_component	extracellular exosome
D	0075342	biological_process	symbiont-mediated disruption of host cell PML body
D	1903901	biological_process	negative regulation of viral life cycle
D	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 401

Chain	Residue
A	ASN161
A	ASP175
A	MG402
A	ACP403
A	HOH502

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 402

Chain	Residue
A	ASP175
A	MG401
A	ACP403

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ACP A 403

Chain	Residue
A	SER51
A	VAL53
A	VAL66
A	LYS68
A	GLU114
A	VAL116
A	ASN161
A	MET163
A	ASP175
A	MG401
A	MG402
A	HOH502
A	LEU45

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 401

Chain	Residue
B	ASP156
B	ASP175
B	MG402
B	ACP404
B	HOH505

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 402

Chain	Residue
B	ASN161
B	ASP175
B	MG401
B	ACP404
B	HOH502

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL B 403

Chain	Residue
A	ASP299
A	ASP302

site_id	AC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ACP B 404

Chain	Residue
B	LEU45
B	SER51
B	VAL53
B	VAL66
B	LYS68
B	ILE95
B	GLU114
B	VAL116
B	ASN161
B	MET163
B	ILE174
B	ASP175
B	MG401
B	MG402
B	HOH502
B	HOH505

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 301

Chain	Residue
C	CYS109
C	CYS114
C	CYS137
C	CYS140

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 301

Chain	Residue
D	CYS109
D	CYS114
D	CYS137
D	CYS140

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGKYSEVFeAinitnnek..........VVVK

Chain	Residue	Details
A	LEU45-LYS68

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKphNVMI

Chain	Residue	Details
A	ILE152-ILE164

site_id	PS00626
Number of Residues	11
Details	RCC1_2 Regulator of chromosome condensation (RCC1) signature 2. FGTGfPHILFM

Chain	Residue	Details
C	PHE159-MET169

site_id	PS01101
Number of Residues	32
Details	CK2_BETA Casein kinase II regulatory subunit signature. CPrVyCenqpmLPIGlsdipgeamVKlyCPkC

Chain	Residue	Details
C	CYS109-CYS140

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	570
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	10
Details	Region: {"description":"Interaction with beta subunit","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	10
Details	Region: {"description":"Interaction with alpha subunit","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Motif: {"description":"KSSR motif","evidences":[{"source":"PubMed","id":"24216761","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)