Structure of PDB 6ega Chain A

Receptor sequence
>6egaA (length=266) Species: 9606 (Homo sapiens) [Search protein sequence]
HSFSFYELKNVTNNFDERPISVGGNKMGEGGVVYKGYVNNTTVAVKKLTT
EELKQQFDQEIKVMAKCQHENLVELLGFSSDDLCLVYVYMPNGSLLDRLS
CLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSANILLDEAFTA
KISDFVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREP
QLLLDIKEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNK
RPDIKKVQQLLQEMTA
3D structure
PDB6ega Conformational flexibility and inhibitor binding to unphosphorylated interleukin-1 receptor-associated kinase 4 (IRAK4).
ChainA
Resolution2.512 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) D136 K138 A140 N141 D154 T158
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 J8A A M192 A211 E233 V236 M237 Y262 Y264 M265 G268 I308 H309 L318 S328 D329 F330 M27 A44 E60 V63 M64 Y87 Y89 M90 G93 I133 H134 L143 S153 D154 F155 PDBbind-CN: -logKd/Ki=6.78,IC50=165.1nM
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:6ega, PDBe:6ega, PDBj:6ega
PDBsum6ega
PubMed30679311
UniProtQ9NWZ3|IRAK4_HUMAN Interleukin-1 receptor-associated kinase 4 (Gene Name=IRAK4)

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