5M4U

ORTHORHOMBIC COMPLEX STRUCTURE OF HUMAN PROTEIN KINASE CK2 CATALYTIC SUBUNIT (ISOFORM CK2ALPHA') WITH THE INHIBITOR 4'-CARBOXY-6,8-CHLORO- FLAVONOL (FLC21)

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	0031507	biological_process	heterochromatin formation
A	0031519	cellular_component	PcG protein complex
A	0032435	biological_process	negative regulation of proteasomal ubiquitin-dependent protein catabolic process
A	0035102	cellular_component	PRC1 complex
A	0042176	biological_process	regulation of protein catabolic process
A	0045893	biological_process	positive regulation of DNA-templated transcription
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	13
Details	binding site for residue 7FC A 401

Chain	Residue
A	ARG48
A	ILE175
A	ASP176
A	HOH542
A	HOH646
A	VAL67
A	LYS69
A	ILE96
A	PHE114
A	GLU115
A	TYR116
A	ILE117
A	MET164

---

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

Chain	Residue
A	TRP34
A	LYS80
A	LYS103
A	HOH717

---

site_id	AC3
Number of Residues	4
Details	binding site for residue GOL A 403

Chain	Residue
A	ARG9
A	ALA10
A	ALA14
A	HOH501

---

site_id	AC4
Number of Residues	5
Details	binding site for residue GOL A 404

Chain	Residue
A	TRP25
A	HIS184
A	GLN187
A	ACT408
A	HOH527

---

site_id	AC5
Number of Residues	6
Details	binding site for residue GOL A 405

Chain	Residue
A	HIS277
A	SER278
A	LYS280
A	HOH505
A	HOH536
A	HOH553

---

site_id	AC6
Number of Residues	7
Details	binding site for residue GOL A 406

Chain	Residue
A	PHE122
A	LYS123
A	HIS161
A	GLU231
A	HOH651
A	HOH672
A	HOH682

---

site_id	AC7
Number of Residues	4
Details	binding site for residue ACT A 407

Chain	Residue
A	GLU15
A	SER18
A	LEU19
A	ASN284

---

site_id	AC8
Number of Residues	4
Details	binding site for residue ACT A 408

Chain	Residue
A	ASP26
A	TYR27
A	GLU28
A	GOL404

---

site_id	AC9
Number of Residues	2
Details	binding site for residue ACT A 409

Chain	Residue
A	ARG192
A	LYS199

---

site_id	AD1
Number of Residues	2
Details	binding site for residue CL A 410

Chain	Residue
A	GLU87
A	ARG90

---

site_id	AD2
Number of Residues	6
Details	binding site for residue SO4 A 411

Chain	Residue
A	ARG81
A	ARG156
A	ASN190
A	HOH552
A	HOH628
A	HOH657

---

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

---