Structure of PDB 6o6q Chain A

Receptor sequence

>6o6qA (length=326) Species: 237561 (Candida albicans SC5314)

HRHNTVQSVSRVYADVLSTKPQSYWDYDDLNIKWNPQENYEILRKLGRGK
YSEVFLGIDLEKREKVVIKVLKPVKRKKIKREISILKNLVDGPNIIAMLD
VVRETPGLIFEHINNIDFRSLYPTFTDYDIRFYMYELLKALDYSHSMGIM
HRDVKPHNVMIDHDKKLLRLIDWGLAEYYHPGTEYNVRVASRYFKGPELL
VDYRLYDYSLDMWSFGCMLASMVFMKEPFFHGKSNTDQLVQIVRVLGSKN
FKKYLEKYNISLGEEYEDIGYYNKRQWVRFMNENNKDLVSQEFLDLIDRL
LRYDHQERLTAKEAMKHAYFDPIRVA

3D structure

• PDB: 6o6q Crystal structure of Cka1p, a casein kinase 2 alpha ortholog from Candida albicans
• Chain: A
• Resolution: 2.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D160 K162 N165 D179 S198
• Catalytic site (residue number reindexed from 1): D153 K155 N158 D172 S191
• 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	A	L49 V57 I120 H164 M167 I178	L46 V54 I113 H157 M160 I171

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

External links

• PDB: RCSB:6o6q, PDBe:6o6q, PDBj:6o6q
• PDBsum: 6o6q
• UniProt: A0A1D8PUA2