Structure of PDB 6eiq Chain B

Receptor sequence
>6eiqB (length=340) Species: 9606 (Homo sapiens) [Search protein sequence]
RKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQ
EWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRN
HLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELS
IIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEV
LLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPA
HILDQAPKARKFFEKLPDGTWNLKYKPPGTRKLHNILGVETGGPGGRRAG
ESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFK
3D structure
PDB6eiq Novel Scaffolds for Dual Specificity Tyrosine-Phosphorylation-Regulated Kinase (DYRK1A) Inhibitors.
ChainB
Resolution2.3 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) D155 K157 N160 D175 S192
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 B6Z B I165 V173 A186 M240 S242 D247 L294 I33 V41 A54 M108 S110 D115 L162 MOAD: Ki=383nM
BindingDB: Ki=383nM,IC50=800nM
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:6eiq, PDBe:6eiq, PDBj:6eiq
PDBsum6eiq
PubMed30095246
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

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