Structure of PDB 8c3q Chain B

Receptor sequence
>8c3qB (length=344) Species: 9606 (Homo sapiens) [Search protein sequence]
YNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWV
AIKIIKNKKAFLNQAQIEVRLLELMNKHDEMKYYIVHLKRHFMFRNHLCL
VFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHC
DLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGM
PYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILD
QAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVETGGPGG
RRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFK
3D structure
PDB8c3q Crystal structure of DYRK1A in complex with rutin
ChainB
Resolution2.32 Å
3D
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
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 RUT B I165 F170 A186 K188 E203 L207 V222 F238 L241 S242 N244 N292 V306 D307 F308 I30 F35 A51 K53 E68 L72 V86 F102 L105 S106 N108 N156 V170 D171 F172
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:8c3q, PDBe:8c3q, PDBj:8c3q
PDBsum8c3q
PubMed
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

[Back to BioLiP]