Structure of PDB 7ajy Chain B

Receptor sequence
>7ajyB (length=328) Species: 9606 (Homo sapiens) [Search protein sequence]
RGSHMIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKN
KKAFLNQAQIEVRLLELMNKHKYYIVHLKRHFMFRNHLCLVFEMLSYNLY
DLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLC
NPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWS
LGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFE
KLPDGTWNLKEYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFK
DLILRMLDYDPKTRIQPYYALQHSFFKK
3D structure
PDB7ajy Structure-Guided Discovery of Potent and Selective DYRK1A Inhibitors.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D287 K289 N292 D307 S324
Catalytic site (residue number reindexed from 1) D141 K143 N146 D161 S178
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 RKZ B F170 A186 K188 F238 L241 L294 V306 D307 F28 A44 K46 F92 L95 L148 V160 D161 BindingDB: IC50=8.0nM
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:7ajy, PDBe:7ajy, PDBj:7ajy
PDBsum7ajy
PubMed33975430
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

[Back to BioLiP]