Structure of PDB 6hnw Chain A

Receptor sequence
>6hnwA (length=328) Species: 9606 (Homo sapiens) [Search protein sequence]
GPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSE
VFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVK
DPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGI
MHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPEL
LVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTE
DLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLD
KLLRYDHQSRLTAREAMEHPYFYTVVKD
3D structure
PDB6hnw Inhibitory Properties of ATP-Competitive Coumestrol and Boldine Are Correlated to Different Modulations of CK2 Flexibility.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D156 K158 N161 D175 S194
Catalytic site (residue number reindexed from 1) D154 K156 N159 D173 S192
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 CUE A L45 V53 V66 K68 F113 V116 M163 I174 D175 L43 V51 V64 K66 F111 V114 M161 I172 D173 MOAD: ic50=200nM
BindingDB: Ki=7670nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:6hnw, PDBe:6hnw, PDBj:6hnw
PDBsum6hnw
PubMed30840451
UniProtP68400|CSK21_HUMAN Casein kinase II subunit alpha (Gene Name=CSNK2A1)

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