Structure of PDB 6k0j Chain A

Receptor sequence
>6k0jA (length=327) Species: 9606 (Homo sapiens) [Search protein sequence]
QVPHDHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNNKRFHR
QAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTFELLSMNLYEL
IKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDAKPENILLKQQGR
SGIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCI
LAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAKNFVSSKGY
PRYCTVTTLSDGSVVLNGGRSRRGKLRGPPESREWGNALKGCDDPLFLDF
LKQCLEWDPAVRMTPGQALRHPWLRAA
3D structure
PDB6k0j Inhibition of dual-specificity tyrosine phosphorylation-regulated kinase 2 perturbs 26S proteasome-addicted neoplastic progression.
ChainA
Resolution2.352 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D348 K350 N353 D368 S385
Catalytic site (residue number reindexed from 1) D137 K139 N142 D157 S174
Enzyme Commision number 2.7.12.1: dual-specificity 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 CQO A F233 V236 A249 L304 E352 L355 D368 F22 V25 A38 L93 E141 L144 D157 MOAD: ic50=13nM
PDBbind-CN: -logKd/Ki=7.89,IC50=13nM
Gene Ontology
Molecular Function
GO:0004672 protein 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:6k0j, PDBe:6k0j, PDBj:6k0j
PDBsum6k0j
PubMed31754034
UniProtQ92630|DYRK2_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 2 (Gene Name=DYRK2)

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