Structure of PDB 1ds5 Chain D Binding Site BS02
Receptor Information
>1ds5 Chain D (length=328) Species:
4577
(Zea mays) [
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MSKARVYADVNVLRPKEYWDYEALTVQWGEQDDYEVVRKVGRGKYSEVFE
GINVNNNEKCIIKILKPVKKKKIKREIKILQNLCGGPNIVKLLDIVRDQH
SKTPSLIFEYVNNTDFKVLYPTLTDYDIRYYIYELLKALDYCHSQGIMHR
DVKPHNVMIDHELRKLRLIDWGLAEFYHPGKEYNVRVASRYFKGPELLVD
LQDYDYSLDMWSLGCMFAGMIFRKEPFFYGHDNHDQLVKIAKVLGTDGLN
VYLNKYRIELDPQLEALVGRHSRKPWLKFMNADNQHLVSPEAIDFLDKLL
RYDHQERLTALEAMTHPYFQQVRAAENS
Ligand information
>1ds5 Chain H (length=16) Species:
9606
(Homo sapiens) [
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YGFKIHPMAYQLQLQA
Receptor-Ligand Complex Structure
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PDB
1ds5
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.
Resolution
3.16 Å
Binding residue
(original residue number in PDB)
Q36 E40 V41 F54 I57 I69 D103
Binding residue
(residue number reindexed from 1)
Q31 E35 V36 F49 I52 I64 D98
Enzymatic activity
Catalytic site (original residue number in PDB)
D156 K158 N161 D175 S194
Catalytic site (residue number reindexed from 1)
D151 K153 N156 D170 S189
Enzyme Commision number
2.7.11.1
: non-specific serine/threonine protein kinase.
Gene Ontology
Molecular Function
GO:0004672
protein kinase activity
GO:0004674
protein serine/threonine kinase activity
GO:0005524
ATP binding
GO:0044024
histone H2AS1 kinase activity
GO:0106310
protein serine kinase activity
Biological Process
GO:0006338
chromatin remodeling
GO:0006468
protein phosphorylation
GO:0016310
phosphorylation
GO:0051726
regulation of cell cycle
Cellular Component
GO:0005634
nucleus
GO:0005829
cytosol
GO:0005956
protein kinase CK2 complex
GO:0043231
intracellular membrane-bounded organelle
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1ds5
,
PDBe:1ds5
,
PDBj:1ds5
PDBsum
1ds5
PubMed
10931203
UniProt
P28523
|CSK2A_MAIZE Casein kinase II subunit alpha (Gene Name=ACK2)
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