4MWH

Crystal structure of scCK2 alpha in complex with ATP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000028	biological_process	ribosomal small subunit assembly
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	0005730	cellular_component	nucleolus
A	0005829	cellular_component	cytosol
A	0005956	cellular_component	protein kinase CK2 complex
A	0006338	biological_process	chromatin remodeling
A	0006356	biological_process	regulation of transcription by RNA polymerase I
A	0006359	biological_process	regulation of transcription by RNA polymerase III
A	0006468	biological_process	protein phosphorylation
A	0006974	biological_process	DNA damage response
A	0007535	biological_process	donor selection
A	0016310	biological_process	phosphorylation
A	0030490	biological_process	maturation of SSU-rRNA
A	0032040	cellular_component	small-subunit processome
A	0032545	cellular_component	CURI complex
A	0034456	cellular_component	UTP-C complex
A	0042790	biological_process	nucleolar large rRNA transcription by RNA polymerase I
A	0044024	molecular_function	histone H2AS1 kinase activity
A	0051726	biological_process	regulation of cell cycle
A	0060962	biological_process	regulation of ribosomal protein gene transcription by RNA polymerase II
A	0106310	molecular_function	protein serine kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ATP A 401

Chain	Residue
A	ARG48
A	GLU153
A	VAL155
A	ASP195
A	LYS197
A	HIS199
A	ASN200
A	MET202
A	ILE213
A	ASP214
A	MG402
A	GLY49
A	SO4407
A	HOH507
A	HOH548
A	HOH563
A	HOH622
A	LYS50
A	TYR51
A	SER52
A	VAL54
A	VAL67
A	LYS69
A	ILE134

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 402

Chain	Residue
A	ASN200
A	ASP214
A	ATP401
A	HOH622

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 403

Chain	Residue
A	HIS187
A	ALA354
A	HOH523
A	HOH554

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 404

Chain	Residue
A	ARG268
A	LYS317
A	ARG321
A	ASN324
A	ASP325

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 405

Chain	Residue
A	ARG161
A	LYS166

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 406

Chain	Residue
A	ARG81
A	ARG194
A	ASN228
A	VAL231
A	HOH513

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 407

Chain	Residue
A	LYS197
A	HIS199
A	ATP401
A	HOH622
A	HOH632

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 408

Chain	Residue
A	ARG234
A	ASN277
A	HOH589

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 409

Chain	Residue
A	ARG316
A	PRO318
A	TRP319
A	HIS320

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL46-LYS69

---

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

Chain	Residue	Details
A	ILE191-ILE203

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP195

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	VAL46
A	LYS69

---