Structure of PDB 6ej4 Chain C

Receptor sequence
>6ej4C (length=332) Species: 9606 (Homo sapiens) [Search protein sequence]
VYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEW
VAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHL
CLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSII
HCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLL
GMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHI
LDQAPKARKFFDGTWNLKKREYKPKLHNILGVETGGPGGRRAGESGHTVA
DYLKFKDLILRMLDYDPKTRIQPYYALQHSFF
3D structure
PDB6ej4 Novel Scaffolds for Dual Specificity Tyrosine-Phosphorylation-Regulated Kinase (DYRK1A) Inhibitors.
ChainC
Resolution2.88 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D287 K289 N292 D307 S324
Catalytic site (residue number reindexed from 1) D153 K155 N158 D173 S190
Enzyme Commision number 2.7.11.23: [RNA-polymerase]-subunit kinase.
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 B7W C I165 V173 A186 L241 S242 Y243 D247 L294 V306 I31 V39 A52 L107 S108 Y109 D113 L160 V172 BindingDB: IC50=329nM,Ki=158nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004712 protein serine/threonine/tyrosine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation
GO:0046777 protein autophosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:6ej4, PDBe:6ej4, PDBj:6ej4
PDBsum6ej4
PubMed30095246
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

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