Structure of PDB 6uip Chain C

Receptor sequence
>6uipC (length=306) Species: 9606 (Homo sapiens) [Search protein sequence]
KERKVYNDGYDDDNYDYIVKNGEKYEIDSLIGKGSFGQVVKAYDWVAIKI
IKNKKAFLNQAQIEVRLLELMNKHIVHRHFMFRNHLCLVFEMLSYNLYDL
LRNTNFRGVSLNLTRKFAQQMCTALLFLATPIIHCDLKPENILLCNPKRS
AIKIVDFGYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPL
FSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWNLKKTRE
YKPPGTRKLHNILGVETGGPGGRRVADYLKFKDLILRMLDYDPKTRIQPY
YALQHS
3D structure
PDB6uip Selective DYRK1A Inhibitor for the Treatment of Type 1 Diabetes: Discovery of 6-Azaindole Derivative GNF2133.
ChainC
Resolution3.7 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) D136 K138 N141 D156 S164
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 Q8J C I165 A186 K188 F238 E239 L241 N292 L294 V306 D307 I31 A47 K49 F90 E91 L93 N141 L143 V155 D156 BindingDB: IC50=6.2nM
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:6uip, PDBe:6uip, PDBj:6uip
PDBsum6uip
PubMed32077280
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

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