Structure of PDB 6uya Chain D

Receptor sequence
>6uyaD (length=291) Species: 9606 (Homo sapiens) [Search protein sequence]
DTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVA
VKKLAAMVDITTEELKQQFDQEIKVMAKCQHENLVELLGFSSDGDDLCLV
YVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRD
IKSANILLDEAFTAKISDFGLARATVMTSRIVGTTAYMAPEALRGEITPK
SDIYSFGVVLLEIITGLPAVDEHREPQLLLDIKEEIEDEEKTIEDYIDKK
MNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMT
3D structure
PDB6uya Discovery of Potent Benzolactam IRAK4 Inhibitors with Robust in Vivo Activity.
ChainD
Resolution1.74 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) D311 K313 A315 N316 D329 T351
Catalytic site (residue number reindexed from 1) D150 K152 A154 N155 D168 T184
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein 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 QL7 D M192 A211 Y262 M265 G268 R273 T280 L318 M31 A50 Y101 M104 G107 R112 T119 L157 BindingDB: Ki=1.50nM,IC50=0.190000nM
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation
GO:0007165 signal transduction

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6uya, PDBe:6uya, PDBj:6uya
PDBsum6uya
PubMed32184965
UniProtQ9NWZ3|IRAK4_HUMAN Interleukin-1 receptor-associated kinase 4 (Gene Name=IRAK4)

[Back to BioLiP]