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BioLiP

Structure of PDB 7b8h Chain A

Receptor sequence
>7b8hA (length=329) Species: 9606 (Homo sapiens) [Search protein sequence]
SGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYS
EVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIV
KDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMG
IMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPE
LLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGT
EDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFL
DKLLRYDHQSRLTAREAMEHPYFYTVVKD
3D structure
PDB7b8h Structural basis for the design of bisubstrate inhibitors of protein kinase CK2 provided by complex structures with the substrate-competitive inhibitor heparin.
ChainA
Resolution1.34 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) D155 K157 N160 D174 S193
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 IDS A K49 R191 K48 R190
BS02 SGN A R191 K198 R190 K197
BS03 SGN A K122 K158 P159 H160 K121 K157 P158 H159
BS04 NIO A K68 F113 I174 D175 K67 F112 I173 D174
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:7b8h, PDBe:7b8h, PDBj:7b8h
PDBsum7b8h
PubMed33571828
UniProtP68400|CSK21_HUMAN Casein kinase II subunit alpha (Gene Name=CSNK2A1)

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