Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5YF9

Crystal structure of CK2a2 form-2

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0000166	molecular_function	nucleotide binding
B	0000785	cellular_component	chromatin
B	0001669	cellular_component	acrosomal vesicle
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005956	cellular_component	protein kinase CK2 complex
B	0006302	biological_process	double-strand break repair
B	0006468	biological_process	protein phosphorylation
B	0006915	biological_process	apoptotic process
B	0006974	biological_process	DNA damage response
B	0007283	biological_process	spermatogenesis
B	0016055	biological_process	Wnt signaling pathway
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0021987	biological_process	cerebral cortex development
B	0031519	cellular_component	PcG protein complex
B	0032435	biological_process	negative regulation of proteasomal ubiquitin-dependent protein catabolic process
B	0042176	biological_process	regulation of protein catabolic process
B	0051726	biological_process	regulation of cell cycle
B	0097421	biological_process	liver regeneration
B	0106310	molecular_function	protein serine kinase activity
B	1901524	biological_process	regulation of mitophagy
B	1903955	biological_process	positive regulation of protein targeting to mitochondrion
B	1905818	biological_process	regulation of chromosome separation
B	2001234	biological_process	negative regulation of apoptotic signaling pathway
X	0000166	molecular_function	nucleotide binding
X	0000785	cellular_component	chromatin
X	0001669	cellular_component	acrosomal vesicle
X	0004672	molecular_function	protein kinase activity
X	0004674	molecular_function	protein serine/threonine kinase activity
X	0005515	molecular_function	protein binding
X	0005524	molecular_function	ATP binding
X	0005634	cellular_component	nucleus
X	0005654	cellular_component	nucleoplasm
X	0005737	cellular_component	cytoplasm
X	0005829	cellular_component	cytosol
X	0005956	cellular_component	protein kinase CK2 complex
X	0006302	biological_process	double-strand break repair
X	0006468	biological_process	protein phosphorylation
X	0006915	biological_process	apoptotic process
X	0006974	biological_process	DNA damage response
X	0007283	biological_process	spermatogenesis
X	0016055	biological_process	Wnt signaling pathway
X	0016301	molecular_function	kinase activity
X	0016740	molecular_function	transferase activity
X	0021987	biological_process	cerebral cortex development
X	0031519	cellular_component	PcG protein complex
X	0032435	biological_process	negative regulation of proteasomal ubiquitin-dependent protein catabolic process
X	0042176	biological_process	regulation of protein catabolic process
X	0051726	biological_process	regulation of cell cycle
X	0097421	biological_process	liver regeneration
X	0106310	molecular_function	protein serine kinase activity
X	1901524	biological_process	regulation of mitophagy
X	1903955	biological_process	positive regulation of protein targeting to mitochondrion
X	1905818	biological_process	regulation of chromosome separation
X	2001234	biological_process	negative regulation of apoptotic signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue NIO X 401

Chain	Residue
X	VAL67
X	LYS69
X	PHE114
X	ILE175
X	ASP176
X	HOH585
X	HOH610
X	HOH621

site_id	AC2
Number of Residues	8
Details	binding site for residue SO4 X 402

Chain	Residue
X	ARG81
X	ARG156
X	ASN190
X	HOH508
X	HOH561
X	HOH712
X	HOH737
X	LYS78

site_id	AC3
Number of Residues	8
Details	binding site for residue SO4 X 403

Chain	Residue
X	ARG307
X	TYR308
X	ASP309
X	HOH560
X	HOH572
X	HOH591
X	HOH626
X	HOH769

site_id	AC4
Number of Residues	3
Details	binding site for residue SO4 X 404

Chain	Residue
X	LYS171
X	ARG173
X	HOH657

site_id	AC5
Number of Residues	5
Details	binding site for residue SO4 X 405

Chain	Residue
X	HIS287
X	SER288
X	ARG291
X	HOH725
X	HOH763

site_id	AC6
Number of Residues	9
Details	binding site for residue SO4 X 406

Chain	Residue
B	ARG192
B	HOH721
X	LYS199
X	ASN239
X	HOH507
X	HOH511
X	HOH535
X	HOH612
X	HOH617

site_id	AC7
Number of Residues	5
Details	binding site for residue NIO B 401

Chain	Residue
B	LYS69
B	PHE114
B	ILE175
B	ASP176
B	HOH549

site_id	AC8
Number of Residues	8
Details	binding site for residue SO4 B 402

Chain	Residue
B	LYS78
B	ARG81
B	ARG156
B	ASN190
B	HOH516
B	HOH521
B	HOH553
B	HOH587

site_id	AC9
Number of Residues	7
Details	binding site for residue SO4 B 403

Chain	Residue
B	ARG307
B	ASP309
B	HOH531
B	HOH564
B	HOH664
B	HOH724
B	HOH744

site_id	AD1
Number of Residues	8
Details	binding site for residue SO4 B 404

Chain	Residue
B	ARG192
B	LYS199
B	ASN239
B	HOH608
B	HOH771
B	HOH786
X	ARG192
X	HOH507

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
X	LEU46-LYS69

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

Chain	Residue	Details
X	ILE153-ILE165

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
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_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
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_FI5
Number of Residues	4
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_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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