Structure of PDB 6o6q Chain B

Receptor sequence
>6o6qB (length=325) Species: 237561 (Candida albicans SC5314) [Search protein sequence]
RHNTVQSVSRVYADVLSTKPQSYWDYDDLNIKWNPQENYEILRKLGRGKY
SEVFLGIDLEKREKVVIKVLKPVKRKKIKREISILKNLVDGPNIIAMLDV
VRKTPGLIFEHINNIDFRSLYPTFTDYDIRFYMYELLKALDYSHSMGIMH
RDVKPHNVMIDHDKKLLRLIDWGLAEYYHPGTEYNVRVASRYFKGPELLV
DYRLYDYSLDMWSFGCMLASMVFMKEPFFHGKSNTDQLVQIVRVLGSKNF
KKYLEKYNISLGEEYEDIGYYNKRQWVRFMNENNKDLVSQEFLDLIDRLL
RYDHQERLTAKEAMKHAYFDPIRVA
3D structure
PDB6o6q Crystal structure of Cka1p, a casein kinase 2 alpha ortholog from Candida albicans
ChainB
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D160 K162 N165 D179 S198
Catalytic site (residue number reindexed from 1) D152 K154 N157 D171 S190
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 AMP B L49 V57 V70 H119 I120 H164 M167 L45 V53 V66 H111 I112 H156 M159
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
GO:0106310 protein serine kinase activity
Biological Process
GO:0006356 regulation of transcription by RNA polymerase I
GO:0006359 regulation of transcription by RNA polymerase III
GO:0006468 protein phosphorylation
GO:0006974 DNA damage response
GO:0016310 phosphorylation
GO:0042273 ribosomal large subunit biogenesis
GO:0051726 regulation of cell cycle
Cellular Component
GO:0005634 nucleus
GO:0005829 cytosol
GO:0005956 protein kinase CK2 complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6o6q, PDBe:6o6q, PDBj:6o6q
PDBsum6o6q
PubMed
UniProtA0A1D8PUA2

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