6HMC

STRUCTURE OF PROTEIN KINASE CK2 CATALYTIC SUBUNIT (ISOFORM CK2ALPHA'; CSNK2A2 gene product) IN COMPLEX WITH THE INDENOINDOLE-TYPE INHIBITOR THN27

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue EDO A 401

Chain	Residue
A	HIS184
A	HOH502

---

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO A 402

Chain	Residue
A	ASP131
A	HIS292
A	VAL294
A	HOH851

---

site_id	AC3
Number of Residues	7
Details	binding site for residue EDO A 403

Chain	Residue
A	ASP300
A	HIS322
A	HOH642
A	HOH682
A	LYS45
A	PRO296
A	GLU297

---

site_id	AC4
Number of Residues	3
Details	binding site for residue EDO A 404

Chain	Residue
A	GLU188
A	ASN190
A	GLN208

---

site_id	AC5
Number of Residues	8
Details	binding site for residue EDO A 405

Chain	Residue
A	LEU42
A	PHE55
A	GLU318
A	GLU321
A	HIS322
A	HOH511
A	HOH527
A	HOH547

---

site_id	AC6
Number of Residues	9
Details	binding site for residue EDO A 406

Chain	Residue
A	GLU64
A	ARG65
A	ASP206
A	ASP265
A	HOH506
A	HOH532
A	HOH536
A	HOH650
A	HOH919

---

site_id	AC7
Number of Residues	9
Details	binding site for residue EDO A 407

Chain	Residue
A	TYR13
A	VAL16
A	VAL106
A	HOH728
A	HOH744
A	HOH764
A	HOH770
A	HOH779
A	HOH896

---

site_id	AC8
Number of Residues	2
Details	binding site for residue EDO A 408

Chain	Residue
A	ARG22
A	GLN237

---

site_id	AC9
Number of Residues	17
Details	binding site for residue FXB A 409

Chain	Residue
A	LEU46
A	VAL54
A	VAL67
A	LYS69
A	ILE96
A	PHE114
A	GLU115
A	ILE117
A	MET164
A	ILE175
A	ASP176
A	HOH514
A	HOH531
A	HOH657
A	HOH722
A	HOH819
A	HOH932

---

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
A	LEU46-LYS69

---

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

Chain	Residue	Details
A	ILE153-ILE165

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	285
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	1
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_FI3
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
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_FI6
Number of Residues	2
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_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---