Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1DS5

DIMERIC CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT IN COMPLEX WITH TWO BETA PEPTIDES MIMICKING THE ARCHITECTURE OF THE TETRAMERIC PROTEIN KINASE CK2 HOLOENZYME.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005829	cellular_component	cytosol
A	0005956	cellular_component	protein kinase CK2 complex
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	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
A	0016740	molecular_function	transferase activity
A	0043231	cellular_component	intracellular membrane-bounded organelle
A	0051726	biological_process	regulation of cell cycle
A	0106310	molecular_function	protein serine kinase activity
B	0000166	molecular_function	nucleotide binding
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005829	cellular_component	cytosol
B	0005956	cellular_component	protein kinase CK2 complex
B	0006356	biological_process	regulation of transcription by RNA polymerase I
B	0006359	biological_process	regulation of transcription by RNA polymerase III
B	0006468	biological_process	protein phosphorylation
B	0006974	biological_process	DNA damage response
B	0016301	molecular_function	kinase activity
B	0016310	biological_process	phosphorylation
B	0016740	molecular_function	transferase activity
B	0043231	cellular_component	intracellular membrane-bounded organelle
B	0051726	biological_process	regulation of cell cycle
B	0106310	molecular_function	protein serine kinase activity
C	0000166	molecular_function	nucleotide binding
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005829	cellular_component	cytosol
C	0005956	cellular_component	protein kinase CK2 complex
C	0006356	biological_process	regulation of transcription by RNA polymerase I
C	0006359	biological_process	regulation of transcription by RNA polymerase III
C	0006468	biological_process	protein phosphorylation
C	0006974	biological_process	DNA damage response
C	0016301	molecular_function	kinase activity
C	0016310	biological_process	phosphorylation
C	0016740	molecular_function	transferase activity
C	0043231	cellular_component	intracellular membrane-bounded organelle
C	0051726	biological_process	regulation of cell cycle
C	0106310	molecular_function	protein serine kinase activity
D	0000166	molecular_function	nucleotide binding
D	0004672	molecular_function	protein kinase activity
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0005524	molecular_function	ATP binding
D	0005634	cellular_component	nucleus
D	0005829	cellular_component	cytosol
D	0005956	cellular_component	protein kinase CK2 complex
D	0006356	biological_process	regulation of transcription by RNA polymerase I
D	0006359	biological_process	regulation of transcription by RNA polymerase III
D	0006468	biological_process	protein phosphorylation
D	0006974	biological_process	DNA damage response
D	0016301	molecular_function	kinase activity
D	0016310	biological_process	phosphorylation
D	0016740	molecular_function	transferase activity
D	0043231	cellular_component	intracellular membrane-bounded organelle
D	0051726	biological_process	regulation of cell cycle
D	0106310	molecular_function	protein serine kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 1001

Chain	Residue
D	HOH1059
D	HOH1070
D	HOH1071
D	HOH1072

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 1002

Chain	Residue
D	HOH1073
D	HOH1074
D	HOH1075

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 1003

Chain	Residue
B	ALA193
B	HOH1073
B	HOH1074
B	HOH1075
B	ARG191
B	VAL192

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 1004

Chain	Residue
B	HOH1065
B	HOH1076
B	HOH1077
B	HOH1078

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP A 501

Chain	Residue
A	VAL45
A	ILE66
A	HIS160
A	ASN161
A	MET163
A	ILE174
A	ASP175
B	ARG47

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE AMP C 601

Chain	Residue
C	VAL45
C	GLY48
C	VAL53
C	ILE66
C	VAL95
C	GLU114
C	VAL116
C	ASN161
C	MET163
C	ILE174
C	ASP175

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE AMP D 701

Chain	Residue
D	SER51
D	VAL53
D	ILE66
D	LYS68
D	GLU114
D	VAL116
D	ASN161
D	MET163
D	ASP175
D	HOH1010
D	HOH1053

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE AMP B 801

Chain	Residue
B	SER51
B	VAL53
B	ILE66
B	LYS68
B	GLU114
B	VAL116
B	HIS160
B	MET163
B	ILE174
B	ASP175

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL45-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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASP156
B	ASP156
C	ASP156
D	ASP156

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
A	VAL45
A	LYS68
B	VAL45
B	LYS68
C	VAL45
C	LYS68
D	VAL45
D	LYS68

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)