Structure of PDB 4ylj Chain A Binding Site BS01

Receptor Information
>4ylj Chain A (length=347) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEW
VAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHL
CLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSII
HCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLL
GMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHI
LDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVETGGP
GGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKK
Ligand information
Ligand ID4E1
InChIInChI=1S/C16H9IN2O2/c17-10-6-3-5-9-12-14(19-13(9)10)8-4-1-2-7-11(8)18-15(12)16(20)21/h1-7,19H,(H,20,21)
InChIKeySDRAETFVRBBLOB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01c32c1nc4c(c1c(nc2cccc3)C(O)=O)cccc4I
OpenEye OEToolkits 1.9.2c1ccc2c(c1)c3c(c4cccc(c4[nH]3)I)c(n2)C(=O)O
CACTVS 3.385OC(=O)c1nc2ccccc2c3[nH]c4c(I)cccc4c13
FormulaC16 H9 I N2 O2
Name10-iodo-11H-indolo[3,2-c]quinoline-6-carboxylic acid
ChEMBLCHEMBL3589662
DrugBank
ZINCZINC000230506524
PDB chain4ylj Chain A Residue 505 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4ylj 10-Iodo-11H-indolo[3,2-c]quinoline-6-carboxylic Acids Are Selective Inhibitors of DYRK1A.
Resolution2.58 Å
Binding residue
(original residue number in PDB)		F170 V173 K188 F238 L241 L294 D307
Binding residue
(residue number reindexed from 1)		F36 V39 K54 F104 L107 L160 D173
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=8.22,IC50=0.006uM
BindingDB: IC50=6.0nM
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.
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:4ylj, PDBe:4ylj, PDBj:4ylj
PDBsum4ylj
PubMed25730262
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

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