Structure of PDB 6eif Chain A

Receptor sequence
>6eifA (length=344) Species: 9606 (Homo sapiens) [Search protein sequence]
KVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQE
WVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNH
LCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSI
IHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVL
LGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAH
ILDQAPKARKFFEKLPDGTWNLKKTKDEYKPPGTRKLHNILGVETGGPGG
RRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFK
3D structure
PDB6eif Novel Scaffolds for Dual Specificity Tyrosine-Phosphorylation-Regulated Kinase (DYRK1A) Inhibitors.
ChainA
Resolution2.22 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) D154 K156 N159 D174 S191
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 B5T A I165 A186 K188 L241 L294 V306 I32 A53 K55 L108 L161 V173 MOAD: Ki=104nM
PDBbind-CN: -logKd/Ki=6.98,Ki=104nM
BindingDB: Ki=104nM,IC50=216nM
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
View graph for
Biological Process
External links
PDB RCSB:6eif, PDBe:6eif, PDBj:6eif
PDBsum6eif
PubMed30095246
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

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