1LR4

Room Temperature Crystal Structure of the Apo-form of the catalytic subunit of protein kinase CK2 from Zea mays

Replaces:  1A6O

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BEN A 1001

Chain	Residue
A	ILE66
A	LYS68
A	PHE113
A	MET163
A	ILE174
A	ASP175
A	HOH1016
A	HOH1065

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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

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASP156

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	LYS68
A	VAL45

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