Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1JWH

Crystal Structure of Human Protein Kinase CK2 Holoenzyme

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	4
Details	BINDING SITE FOR RESIDUE PO4 A 350

Chain	Residue
A	HIS234
A	ARG244
A	HOH394
A	HOH397

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 B 351

Chain	Residue
B	ARG244
B	HOH365

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 352

Chain	Residue
B	HOH375
B	ARG195
B	LYS198
B	ASN238

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 353

Chain	Residue
C	LYS147
C	SER148
C	ARG150
C	HOH358
C	HOH366

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 D 354

Chain	Residue
D	ARG17
D	SER148
D	SER149
D	PO4355
D	HOH359
D	HOH364

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 D 355

Chain	Residue
C	GLU57
D	LYS147
D	ARG150
D	PO4354

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 D 356

Chain	Residue
D	GLU20
D	LYS100
D	ASP105
D	HOH361

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C 357

Chain	Residue
C	CYS109
C	CYS114
C	CYS137
C	CYS140
C	TYR144

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN D 358

Chain	Residue
D	CYS109
D	CYS114
D	CYS137
D	CYS140
D	TYR144

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ANP A 340

Chain	Residue
A	SER51
A	VAL66
A	LYS68
A	GLU114
A	VAL116
A	HIS160
A	MET163
A	ASP175
A	HOH384

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	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

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"11574463","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP156
A	HIS160

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP156
B	HIS160

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP156
A	LYS158

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP156
B	LYS158

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP156
A	LYS158
A	SER194

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP156
B	LYS158
B	SER194

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP156
A	ASN161
A	LYS158

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP156
B	ASN161
B	LYS158

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