Structure of PDB 2oic Chain A

Receptor sequence
>2oicA (length=279) Species: 9606 (Homo sapiens) [Search protein sequence]
TRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAV
KKLKQQFDQEIKVMAKCQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDR
LSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSANILLDEAF
TAKISDFGLARATVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLE
IITGLPAVDEHREPQLLLDIKEEIEDEEKTIEDYIDKKMNDADSTSVEAM
YSVASQCLHEKKNKRPDIKKVQQLLQEMT
3D structure
PDB2oic Cutting Edge: IL-1 Receptor-Associated Kinase 4 Structures Reveal Novel Features and Multiple Conformations.
ChainA
Resolution2.4 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) D138 K140 A142 N143 D156 T172
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 STU A M192 E194 G195 V200 A211 Y264 M265 G268 A315 N316 L318 M30 E32 G33 V38 A49 Y91 M92 G95 A142 N143 L145 MOAD: ic50=4nM
PDBbind-CN: -logKd/Ki=8.40,IC50=4nM
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:2oic, PDBe:2oic, PDBj:2oic
PDBsum2oic
PubMed17312103
UniProtQ9NWZ3|IRAK4_HUMAN Interleukin-1 receptor-associated kinase 4 (Gene Name=IRAK4)

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