Structure of PDB 6tia Chain A

Receptor sequence
>6tiaA (length=288) Species: 9606 (Homo sapiens) [Search protein sequence]
TRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAV
KKLAAITTEELKQQFDQEIKVMAKCQHENLVELLGFSSDGDDLCLVYVYM
PNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSA
NILLDEAFTAKISDFGLARASVMTSRIVGTTAYMAPEALRGEITPKSDIY
SFGVVLLEIITGLPAVDEHREPQLLLDIKEEIEDEEKTIEDYIDKKMNDA
DSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTA
3D structure
PDB6tia Improving metabolic stability and removing aldehyde oxidase liability in a 5-azaquinazoline series of IRAK4 inhibitors.
ChainA
Resolution2.52 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D311 K313 A315 N316 D329 T351
Catalytic site (residue number reindexed from 1) D146 K148 A150 N151 D164 T180
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 ND2 A M192 G193 V200 A211 Y262 Y264 M265 G268 S269 R273 D278 T280 L318 S328 M30 G31 V38 A49 Y97 Y99 M100 G103 S104 R108 D113 T115 L153 S163
BS02 ND2 A K227 F230 D231 I234 K235 A238 F251 S253 K62 F65 D66 I69 K70 A73 F86 S88
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

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Molecular Function
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Biological Process
External links
PDB RCSB:6tia, PDBe:6tia, PDBj:6tia
PDBsum6tia
PubMed33091850
UniProtQ9NWZ3|IRAK4_HUMAN Interleukin-1 receptor-associated kinase 4 (Gene Name=IRAK4)

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