M00197
type: Enzyme
rlcp: p1165
cath: Phosphorylase Kinase; domain 1
cath: Transferase(Phosphotransferase); domain 1
cath: protein kinase ck2 holoenzyme, chain C, domain 1
cath: N-terminal domain of TfIIb
ec: https://purl.uniprot.org/enzyme/2.7.11.1
uniprot: P28020
uniprot: P68400
uniprot: Q6INV5
uniprot: P19784
uniprot: P28021
uniprot: P67870
kegg enzyme: Non-specific serine/threonine protein kinase
kegg cofactor: Magnesium
kegg cofactor: Zinc
kegg substrate: ATP
kegg substrate: Protein
kegg product: ADP
kegg product: Phosphoprotein
pdb: 1jwhA01
pdb: 1jwhB01
pdb: 1na7A01
pdb: 1pjkA01
pdb: 1ymiA02
pdb: 2pvrA02
pdb: 2zjwA02
pdb: 3bqcA02
pdb: 3c13A02
pdb: 3fwqA02
pdb: 3fwqB02
pdb: 3h30A02
pdb: 3h30B02
pdb: 3juhA02
pdb: 3juhB02
pdb: 3mb6A02
pdb: 3mb7A02
pdb: 3ngaA02
pdb: 3ngaB02
pdb: 3nszA02
pdb: 3e3bX02
pdb: 3ofmA02
pdb: 1jwhA02
pdb: 1jwhB02
pdb: 1na7A02
pdb: 1pjkA02
pdb: 1ymiA01
pdb: 2pvrA01
pdb: 2zjwA01
pdb: 3bqcA01
pdb: 3c13A01
pdb: 3fwqA01
pdb: 3fwqB01
pdb: 3h30A01
pdb: 3h30B01
pdb: 3juhA01
pdb: 3juhB01
pdb: 3mb6A01
pdb: 3mb7A01
pdb: 3ngaA01
pdb: 3ngaB01
pdb: 3nszA01
pdb: 3e3bX01
pdb: 3ofmA01
pdb: 1rqfA01
pdb: 1rqfB01
pdb: 1rqfD01
pdb: 1rqfE01
pdb: 1rqfG01
pdb: 1rqfH01
pdb: 1rqfJ01
pdb: 1rqfK01
pdb: 1jwhC01
pdb: 1jwhD01
pdb: 1qf8A01
pdb: 1qf8B01
pdb: 3eedA01
pdb: 3eedB01
pdb: 1rqfA02
pdb: 1rqfB02

Phosphorylase Kinase; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.200.20
catalytic domain: index.html

Transferase(Phosphotransferase); domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.510.10
catalytic domain: index.html

protein kinase ck2 holoenzyme, chain C, domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.1820.10

N-terminal domain of TfIIb
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.20.25.20

Magnesium
type: KeggCofactor
references: KEGG:C00305
compound type: divalent metal (Ca2+, Mg2+)
references: CHEBI:18420
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Zinc
type: KeggCofactor
references: KEGG:C00038
compound type: heavy metal
references: CHEBI:29105
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

ATP
type: KeggSubstrate
references: KEGG:C00002
compound type: amine group
compound type: nucleotide
references: CHEBI:15422
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Protein
type: KeggSubstrate
references: KEGG:C00017
compound type: peptide/protein

ADP
type: KeggProduct
references: KEGG:C00008
compound type: amine group
compound type: nucleotide
references: CHEBI:16761
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Phosphoprotein
type: KeggProduct
references: KEGG:C00562
compound type: peptide/protein
compound type: phosphate group/phosphate ion

1jwhA01
type: Pdb
references: 1jwh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jwh
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

1jwhB01
type: Pdb
references: 1jwh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jwh
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

1na7A01
type: Pdb
references: 1na7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1na7
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51
comment: mutant E27A, K76N

1pjkA01
type: Pdb
references: 1pjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pjk
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

1ymiA02
type: Pdb
references: 1ymi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ymi
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51
comment: mutant V66A

2pvrA02
type: Pdb
references: 2pvr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2pvr
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

2zjwA02
type: Pdb
references: 2zjw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zjw
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

3bqcA02
type: Pdb
references: 3bqc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3bqc
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

3c13A02
type: Pdb
references: 3c13
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3c13
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

3fwqA02
type: Pdb
references: 3fwq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3fwq
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

3fwqB02
type: Pdb
references: 3fwq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3fwq
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

3h30A02
type: Pdb
references: 3h30
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3h30
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

3h30B02
type: Pdb
references: 3h30
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3h30
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

3juhA02
type: Pdb
references: 3juh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3juh
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

3juhB02
type: Pdb
references: 3juh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3juh
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

3mb6A02
type: Pdb
references: 3mb6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3mb6
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

3mb7A02
type: Pdb
references: 3mb7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3mb7
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

3ngaA02
type: Pdb
references: 3nga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3nga
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

3ngaB02
type: Pdb
references: 3nga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3nga
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

3nszA02
type: Pdb
references: 3nsz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3nsz
catalytic residue: LYS 68
main chain in catalysis: LYS 49;TYR 50;SER 51

3e3bX02
type: Pdb
references: 3e3b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3e3b
catalytic residue: LYS 69
main chain in catalysis: LYS 50;TYR 51;SER 52

3ofmA02
type: Pdb
references: 3ofm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ofm
catalytic residue: LYS 69
main chain in catalysis: LYS 50;TYR 51;SER 52

1jwhA02
type: Pdb
references: 1jwh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jwh
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

1jwhB02
type: Pdb
references: 1jwh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jwh
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

1na7A02
type: Pdb
references: 1na7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1na7
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

1pjkA02
type: Pdb
references: 1pjk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pjk
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

1ymiA01
type: Pdb
references: 1ymi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ymi
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
comment: mutant M163L

2pvrA01
type: Pdb
references: 2pvr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2pvr
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

2zjwA01
type: Pdb
references: 2zjw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zjw
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

3bqcA01
type: Pdb
references: 3bqc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3bqc
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

3c13A01
type: Pdb
references: 3c13
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3c13
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

3fwqA01
type: Pdb
references: 3fwq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3fwq
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

3fwqB01
type: Pdb
references: 3fwq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3fwq
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

3h30A01
type: Pdb
references: 3h30
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3h30
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

3h30B01
type: Pdb
references: 3h30
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3h30
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

3juhA01
type: Pdb
references: 3juh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3juh
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

3juhB01
type: Pdb
references: 3juh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3juh
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

3mb6A01
type: Pdb
references: 3mb6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3mb6
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

3mb7A01
type: Pdb
references: 3mb7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3mb7
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

3ngaA01
type: Pdb
references: 3nga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3nga
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

3ngaB01
type: Pdb
references: 3nga
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3nga
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

3nszA01
type: Pdb
references: 3nsz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3nsz
catalytic residue: ASP 156;LYS 158
cofactor binding residue: ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)

3e3bX01
type: Pdb
references: 3e3b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3e3b
catalytic residue: ASP 157;LYS 159
cofactor binding residue: ASN 162(Magnesium-2 binding);ASP 176(Magnesium-1 binding)

3ofmA01
type: Pdb
references: 3ofm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ofm
catalytic residue: ASP 157;LYS 159
cofactor binding residue: ASN 162(Magnesium-2 binding);ASP 176(Magnesium-1 binding)

1rqfB01
type: Pdb
references: 1rqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rqf
comment: invisible 59-66

1rqfD01
type: Pdb
references: 1rqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rqf
comment: invisible 59-65

1rqfG01
type: Pdb
references: 1rqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rqf
comment: invisible 59-67

1rqfH01
type: Pdb
references: 1rqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rqf
comment: invisible 59-67

1rqfK01
type: Pdb
references: 1rqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rqf
comment: invisible 59-66

1qf8A01
type: Pdb
references: 1qf8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qf8
comment: invisible 60-65

1qf8B01
type: Pdb
references: 1qf8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qf8
comment: invisible 59-66

3eedA01
type: Pdb
references: 3eed
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3eed
comment: invisible 60-64

3eedB01
type: Pdb
references: 3eed
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3eed
comment: invisible 60-64

1rqfA02
type: Pdb
references: 1rqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rqf
cofactor binding residue: CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)

1rqfB02
type: Pdb
references: 1rqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rqf
cofactor binding residue: CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)

1rqfD02
type: Pdb
references: 1rqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rqf
cofactor binding residue: CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)

1rqfE02
type: Pdb
references: 1rqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rqf
cofactor binding residue: CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)

1rqfG02
type: Pdb
references: 1rqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rqf
cofactor binding residue: CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)

1rqfH02
type: Pdb
references: 1rqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rqf
cofactor binding residue: CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)

1rqfJ02
type: Pdb
references: 1rqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rqf
cofactor binding residue: CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)

1rqfK02
type: Pdb
references: 1rqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rqf
cofactor binding residue: CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)

1jwhC02
type: Pdb
references: 1jwh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jwh
cofactor binding residue: CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)

1jwhD02
type: Pdb
references: 1jwh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jwh
cofactor binding residue: CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)

1qf8A02
type: Pdb
references: 1qf8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qf8
cofactor binding residue: CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)

1qf8B02
type: Pdb
references: 1qf8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qf8
cofactor binding residue: CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)

3eedA02
type: Pdb
references: 3eed
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3eed
cofactor binding residue: CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)

3eedB02
type: Pdb
references: 3eed
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3eed
cofactor binding residue: CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)

Analogue
compound: ATP
pdb: 1jwhA01
ligand het code: ANP

Analogue
compound: ATP
pdb: 1pjkA01
ligand het code: ANP

Analogue
compound: ATP
pdb: 1ymiA02
ligand het code: ANP

Analogue
compound: ATP
pdb: 2pvrA02
ligand het code: ANP

Analogue
compound: ATP
pdb: 3juhA02
ligand het code: ANP

Analogue
compound: ATP
pdb: 3juhB02
ligand het code: ANP

Analogue
compound: ADP
pdb: 3nszA02
ligand het code: ANP

Protein kinase CK2 structure-function relationship: effects of the beta subunit on reconstitution and activity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7735313
journal: Cell Mol Biol Res
volume: 40
pages: 391-9
published year: 1994
authors:
  item: Boldyreff B
  item: Meggio F
  item: Pinna LA
  item: Issinger OG

Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)
medline id: 98232491
references: http://www.ncbi.nlm.nih.gov/pubmed/9564028
journal: EMBO J
volume: 17
pages: 2451-62
published year: 1998
authors:
  item: Niefind K
  item: Guerra B
  item: Pinna LA
  item: Issinger OG
  item: Schomburg D
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P28523

Crystal structure of the human protein kinase CK2 regulatory subunit reveals its zinc finger-mediated dimerization.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10357806
journal: EMBO J
volume: 18
pages: 2930-40
published year: 1999
authors:
  item: Chantalat L
  item: Leroy D
  item: Filhol O
  item: Nueda A
  item: Benitez MJ
  item: Chambaz EM
  item: Cochet C
  item: Dideberg O
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

GTP plus water mimic ATP in the active site of protein kinase CK2.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10581548
journal: Nat Struct Biol
volume: 6
pages: 1100-3
published year: 1999
authors:
  item: Niefind K
  item: Putter M
  item: Guerra B
  item: Issinger OG
  item: Schomburg D
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystallization and preliminary characterization of crystals of human protein kinase CK2.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337, AND SUBUNIT.
references: http://www.ncbi.nlm.nih.gov/pubmed/11092945
journal: Acta Crystallogr D Biol Crystallogr
volume: 56
pages: 1680-4
published year: 2000
authors:
  item: Niefind K
  item: Guerra B
  item: Ermakowa I
  item: Issinger OG
references: P68400
references: P67870

The crystal structure of the complex of Zea mays alpha subunit with a fragment of human beta subunit provides the clue to the architecture of protein kinase CK2 holoenzyme.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10931203
journal: Eur J Biochem
volume: 267
pages: 5184-90
published year: 2000
authors:
  item: Battistutta R
  item: Sarno S
  item: De Moliner E
  item: Marin O
  item: Issinger OG
  item: Zanotti G
  item: Pinna LA
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The replacement of ATP by the competitive inhibitor emodin induces conformational modifications in the catalytic site of protein kinase CK2.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10882732
journal: J Biol Chem
volume: 275
pages: 29618-22
published year: 2000
authors:
  item: Battistutta R
  item: Sarno S
  item: De Moliner E
  item: Papinutto E
  item: Zanotti G
  item: Pinna LA
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11574463
journal: EMBO J
volume: 20
pages: 5320-31
published year: 2001
authors:
  item: Niefind K
  item: Guerra B
  item: Ermakowa I
  item: Issinger OG
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structural features underlying selective inhibition of protein kinase CK2 by ATP site-directed tetrabromo-2-benzotriazole.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11604527
journal: Protein Sci
volume: 10
pages: 2200-6
published year: 2001
authors:
  item: Battistutta R
  item: De Moliner E
  item: Sarno S
  item: Zanotti G
  item: Pinna LA
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Role of the carboxyl terminus on the catalytic activity of protein kinase CK2alpha subunit.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12417343
journal: FEBS Lett
volume: 531
pages: 363-8
published year: 2002
authors:
  item: Tapia J
  item: Jacob G
  item: Allende CC
  item: Allende JE

Unique activation mechanism of protein kinase CK2. The N-terminal segment is essential for constitutive activity of the catalytic subunit but not of the holoenzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11956194
journal: J Biol Chem
volume: 277
pages: 22509-14
published year: 2002
authors:
  item: Sarno S
  item: Ghisellini P
  item: Pinna LA

Three-dimensional atomic structure of a catalytic subunit mutant of human protein kinase CK2.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-329.
references: http://www.ncbi.nlm.nih.gov/pubmed/14646071
journal: Acta Crystallogr D Biol Crystallogr
volume: 59
pages: 2133-9
published year: 2003
authors:
  item: Pechkova E
  item: Zanotti G
  item: Nicolini C
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P68400

Protein kinase CK2: structure, regulation and role in cellular decisions of life and death.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12396231
journal: Biochem J
volume: 369
pages: 1-15
published year: 2003
authors:
  item: Litchfield DW

Biochemical and three-dimensional-structural study of the specific inhibition of protein kinase CK2 by [5-oxo-5,6-dihydroindolo-(1,2-a)quinazolin-7-yl]acetic acid (IQA).
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/12816539
journal: Biochem J
volume: 374
pages: 639-46
published year: 2003
authors:
  item: Sarno S
  item: de Moliner E
  item: Ruzzene M
  item: Pagano MA
  item: Battistutta R
  item: Bain J
  item: Fabbro D
  item: Schoepfer J
  item: Elliott M
  item: Furet P
  item: Meggio F
  item: Zanotti G
  item: Pinna LA
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structural basis of regulation and substrate specificity of protein kinase CK2 deduced from the modeling of protein-protein interactions.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12740046
journal: BMC Struct Biol
volume: 3
pages: 4
published year: 2003
authors:
  item: Rekha N
  item: Srinivasan N

Inhibition of protein kinase CK2 by anthraquinone-related compounds. A structural insight.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/12419810
journal: J Biol Chem
volume: 278
pages: 1831-6
published year: 2003
authors:
  item: De Moliner E
  item: Moro S
  item: Sarno S
  item: Zagotto G
  item: Zanotti G
  item: Pinna LA
  item: Battistutta R
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-335.
references: http://www.ncbi.nlm.nih.gov/pubmed/12860116
journal: J Mol Biol
volume: 330
pages: 925-34
published year: 2003
authors:
  item: Ermakova I
  item: Boldyreff B
  item: Issinger OG
  item: Niefind K
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P68400

Structure of the regulatory subunit of CK2 in the presence of a p21WAF1 peptide demonstrates flexibility of the acidic loop.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/15388915
journal: Acta Crystallogr D Biol Crystallogr
volume: 60
pages: 1698-704
published year: 2004
authors:
  item: Bertrand L
  item: Sayed MF
  item: Pei XY
  item: Parisini E
  item: Dhanaraj V
  item: Bolanos-Garcia VM
  item: Allende JE
  item: Blundell TL
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Inspecting the structure-activity relationship of protein kinase CK2 inhibitors derived from tetrabromo-benzimidazole.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/16298300
journal: Chem Biol
volume: 12
pages: 1211-9
published year: 2005
authors:
  item: Battistutta R
  item: Mazzorana M
  item: Sarno S
  item: Kazimierczuk Z
  item: Zanotti G
  item: Pinna LA
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/15740749
journal: J Mol Biol
volume: 347
pages: 399-414
published year: 2005
authors:
  item: Yde CW
  item: Ermakova I
  item: Issinger OG
  item: Niefind K
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Primary and secondary interactions between CK2alpha and CK2beta lead to ring-like structures in the crystals of the CK2 holoenzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16335523
journal: Mol Cell Biochem
volume: 274
pages: 3-14
published year: 2005
authors:
  item: Niefind K
  item: Issinger OG

A global view of CK2 function and regulation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16342414
journal: Mol Cell Biochem
volume: 274
pages: 163-70
published year: 2005
authors:
  item: Poole A
  item: Poore T
  item: Bandhakavi S
  item: McCann RO
  item: Hanna DE
  item: Glover CV

Discrimination between the activity of protein kinase CK2 holoenzyme and its catalytic subunits.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16806200
journal: FEBS Lett
volume: 580
pages: 3948-52
published year: 2006
authors:
  item: Salvi M
  item: Sarno S
  item: Marin O
  item: Meggio F
  item: Itarte E
  item: Pinna LA

Evolved to be active: sulfate ions define substrate recognition sites of CK2alpha and emphasise its exceptional role within the CMGC family of eukaryotic protein kinases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/17524418
journal: J Mol Biol
volume: 370
pages: 427-38
published year: 2007
authors:
  item: Niefind K
  item: Yde CW
  item: Ermakova I
  item: Issinger OG
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The CK2 alpha/CK2 beta interface of human protein kinase CK2 harbors a binding pocket for small molecules.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/18291315
journal: Chem Biol
volume: 15
pages: 111-7
published year: 2008
authors:
  item: Raaf J
  item: Brunstein E
  item: Issinger OG
  item: Niefind K
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The catalytic subunit of human protein kinase CK2 structurally deviates from its maize homologue in complex with the nucleotide competitive inhibitor emodin.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/18242640
journal: J Mol Biol
volume: 377
pages: 1-8
published year: 2008
authors:
  item: Raaf J
  item: Klopffleisch K
  item: Issinger OG
  item: Niefind K
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The interaction of CK2alpha and CK2beta, the subunits of protein kinase CK2, requires CK2beta in a preformed conformation and is enthalpically driven.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/18824508
journal: Protein Sci
volume: 17
pages: 2180-6
published year: 2008
authors:
  item: Raaf J
  item: Brunstein E
  item: Issinger OG
  item: Niefind K
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structure of human protein kinase CK2 alpha 2 with a potent indazole-derivative inhibitor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/19193990
journal: Acta Crystallogr Sect F Struct Biol Cryst Commun
volume: 65
pages: 75-9
published year: 2009
authors:
  item: Nakaniwa T
  item: Kinoshita T
  item: Sekiguchi Y
  item: Tada T
  item: Nakanishi I
  item: Kitaura K
  item: Suzuki Y
  item: Ohno H
  item: Hirasawa A
  item: Tsujimoto G
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

First inactive conformation of CK2 alpha, the catalytic subunit of protein kinase CK2.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/19361447
journal: J Mol Biol
volume: 386
pages: 1212-21
published year: 2009
authors:
  item: Raaf J
  item: Issinger OG
  item: Niefind K
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structural insight into human CK2alpha in complex with the potent inhibitor ellagic acid.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/19414254
journal: Bioorg Med Chem Lett
volume: 19
pages: 2920-3
published year: 2009
authors:
  item: Sekiguchi Y
  item: Nakaniwa T
  item: Kinoshita T
  item: Nakanishi I
  item: Kitaura K
  item: Hirasawa A
  item: Tsujimoto G
  item: Tada T
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

New potent dual inhibitors of CK2 and Pim kinases: discovery and structural insights.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/20400536
journal: FASEB J
volume: 24
pages: 3171-85
published year: 2010
authors:
  item: Lopez-Ramos M
  item: Prudent R
  item: Moucadel V
  item: Sautel CF
  item: Barette C
  item: Lafanechere L
  item: Mouawad L
  item: Grierson D
  item: Schmidt F
  item: Florent JC
  item: Filippakopoulos P
  item: Bullock AN
  item: Knapp S
  item: Reiser JB
  item: Cochet C
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structural basis of CX-4945 binding to human protein kinase CK2.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/21093442
journal: FEBS Lett
volume: 585
pages: 104-10
published year: 2011
authors:
  item: Ferguson AD
  item: Sheth PR
  item: Basso AD
  item: Paliwal S
  item: Gray K
  item: Fischmann TO
  item: Le HV
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structure of the human protein kinase CK2 catalytic subunit CK2alpha' and interaction thermodynamics with the regulatory subunit CK2beta.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/21241709
journal: J Mol Biol
volume: 407
pages: 1-12
published year: 2011
authors:
  item: Bischoff N
  item: Olsen B
  item: Raaf J
  item: Bretner M
  item: Issinger OG
  item: Niefind K
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

A-kinase
type: KeggEnzyme

AP50 kinase
type: KeggEnzyme

ATP-protein transphosphorylase
type: KeggEnzyme

Calcium-dependent protein kinase C
type: KeggEnzyme

Calcium/phospholipid-dependent protein kinase
type: KeggEnzyme

cAMP-dependent protein kinase
type: KeggEnzyme

cAMP-dependent protein kinase A
type: KeggEnzyme

Casein kinase
type: KeggEnzyme

Casein kinase (phosphorylating)
type: KeggEnzyme

Casein kinase 2
type: KeggEnzyme

Casein kinase I
type: KeggEnzyme

Casein kinase II
type: KeggEnzyme

cGMP-dependent protein kinase
type: KeggEnzyme

CK-2
type: KeggEnzyme

CKI
type: KeggEnzyme

CKII
type: KeggEnzyme

Cyclic AMP-dependent protein kinase
type: KeggEnzyme

Cyclic AMP-dependent protein kinase A
type: KeggEnzyme

Cyclic monophosphate-dependent protein kinase
type: KeggEnzyme

Cyclic nucleotide-dependent protein kinase
type: KeggEnzyme

Cyclin-dependent kinase
type: KeggEnzyme

Cytidine 3',5'-cyclic monophosphate-responsive protein kinase
type: KeggEnzyme

dsk1
type: KeggEnzyme

Glycogen synthase a kinase
type: KeggEnzyme

Glycogen synthase kinase
type: KeggEnzyme

HIPK2
type: KeggEnzyme

Hpr kinase
type: KeggEnzyme

Hydroxyalkyl-protein kinase
type: KeggEnzyme

Hydroxyalkyl-protein kinase
type: KeggEnzyme

M phase-specific cdc2 kinase
type: KeggEnzyme

Mitogen-activated S6 kinase
type: KeggEnzyme

p82 kinase
type: KeggEnzyme

Phosphorylase b kinase kinase
type: KeggEnzyme

PKA
type: KeggEnzyme

Protein glutamyl kinase
type: KeggEnzyme

Protein kinase (phosphorylating)
type: KeggEnzyme

Protein kinase A
type: KeggEnzyme

Protein kinase CK2
type: KeggEnzyme

Protein kinase p58
type: KeggEnzyme

Protein phosphokinase
type: KeggEnzyme

Protein serine kinase
type: KeggEnzyme

Protein serine-threonine kinase
type: KeggEnzyme

Protein-aspartyl kinase
type: KeggEnzyme

Protein-cysteine kinase
type: KeggEnzyme

Protein-serine kinase
type: KeggEnzyme

Prp4 protein kinase
type: KeggEnzyme

Raf kinase
type: KeggEnzyme

Raf-1
type: KeggEnzyme

Ribosomal protein S6 kinase II
type: KeggEnzyme

Ribosomal S6 protein kinase
type: KeggEnzyme

Serine kinase
type: KeggEnzyme

Serine protein kinase
type: KeggEnzyme

Serine-specific protein kinase
type: KeggEnzyme

Serine(threonine) protein kinase
type: KeggEnzyme

Serine/threonine protein kinase
type: KeggEnzyme

STK32
type: KeggEnzyme

T-antigen kinase
type: KeggEnzyme

Threonine-specific protein kinase
type: KeggEnzyme

Twitchin kinase
type: KeggEnzyme

Type-2 casein kinase
type: KeggEnzyme

betaIIPKC
type: KeggEnzyme

epsilon PKC
type: KeggEnzyme

Wee 1-like kinase
type: KeggEnzyme

Wee-kinase
type: KeggEnzyme

WEE1Hu
type: KeggEnzyme