Structure of PDB 6eij Chain D Binding Site BS01

Receptor Information
>6eij Chain D (length=339) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQE
WVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNH
LCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSI
IHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVL
LGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAH
ILDQAPKARKFFEKLPDGTWNLKKYKPPGTRKLHNILGVETGGPGGRRAG
ESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFF
Ligand information
Ligand IDB5Z
InChIInChI=1S/C23H26N6O3S/c30-20(15-4-5-15)28-23-27-19-7-6-18(26-21(19)33-23)16-2-1-3-17(14-16)25-22(31)24-8-9-29-10-12-32-13-11-29/h1-3,6-7,14-15H,4-5,8-13H2,(H2,24,25,31)(H,27,28,30)
InChIKeyNVIJYBFQLMPXOI-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.6c1cc(cc(c1)NC(=O)NCCN2CCOCC2)c3ccc4c(n3)sc(n4)NC(=O)C5CC5
CACTVS 3.385O=C(NCCN1CCOCC1)Nc2cccc(c2)c3ccc4nc(NC(=O)C5CC5)sc4n3
FormulaC23 H26 N6 O3 S
Name~{N}-[5-[3-(2-morpholin-4-ylethylcarbamoylamino)phenyl]-[1,3]thiazolo[5,4-b]pyridin-2-yl]cyclopropanecarboxamide
ChEMBLCHEMBL4171209
DrugBank
ZINC
PDB chain6eij Chain D Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6eij Novel Scaffolds for Dual Specificity Tyrosine-Phosphorylation-Regulated Kinase (DYRK1A) Inhibitors.
Resolution2.42 Å
Binding residue
(original residue number in PDB)		I165 F170 A186 K188 F238 L241 S242 Y243 L294 D307 S310
Binding residue
(residue number reindexed from 1)		I32 F37 A53 K55 F105 L108 S109 Y110 L161 D174 S177
Annotation score1
Binding affinityMOAD: Ki=1680nM
BindingDB: Ki=1680nM,IC50=3500nM
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.
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6eij, PDBe:6eij, PDBj:6eij
PDBsum6eij
PubMed30095246
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

[Back to BioLiP]