Structure of PDB 4im3 Chain A

Receptor sequence
>4im3A (length=605) Species: 9606 (Homo sapiens) [Search protein sequence]
GSMQSTSNHLWLLSDILGQGATANVFRGRHKKTGDLFAIKVFNNRPVDVQ
MREFEVLKKLNHKNIVKLFAIEEETTTRHKVLIMEFCPCGSLYTVLEEPS
NAYGLPESEFLIVLRDVVGGMNHLRENGIVHRNIKPGNIMRVIGEDGQSV
YKLTDFGATVDLWSIGVTFYHAATGSLPFRPFEGPRRNKEVMYKIITGKP
SGAISGVQKAENGPIDWSGDMPVSCSLSRGLQVLLTPVLANILEADQEKC
WGFDQFFAETSDILHRMVIHVFSLQQMTAHKIYIHSYNTATIFHELVYKQ
TKIISSNQELIYEGRRLVLEPGRLAQHFPKTTEENPIFVVSREPLNTIGL
IYEKISLPKVHPRYDLDGDASMAKAITGVVCYACRIASTLLLYQELMRKG
IRWLIELIKDDYNETVHKKTEVVITLDFCIRNIEKTVKVAAELGEISDIH
TKLLRLSSSQGTIETSLQDIDSRLSPGGSLADAWAHQEGTHPKDRNVEKL
QVLLNCMTEIYYQFKKDKAERRLAYNEEQIHKFDKQKLYYHATKAMTHFT
DECVKKYEAFLNKSEEWIRKMLHLRKQLLSLTNQCFDIEEEVSKYQEYTN
ELQET
3D structure
PDB4im3 Structure and ubiquitination-dependent activation of TANK-binding kinase 1.
ChainA
Resolution3.342 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N135 K137 N140 D157
Catalytic site (residue number reindexed from 1) N133 K135 N138 D155
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 BX7 A G18 A36 K38 M86 F88 C89 G92 T96 M142 T156 D157 G20 A38 K40 M84 F86 C87 G90 T94 M140 T154 D155 BindingDB: IC50=8.0nM,Kd=158nM
Gene Ontology
Molecular Function
GO:0003676 nucleic acid binding
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0019903 protein phosphatase binding
GO:0042802 identical protein binding
GO:0044024 histone H2AS1 kinase activity
GO:0051219 phosphoprotein binding
GO:0106310 protein serine kinase activity
Biological Process
GO:0002218 activation of innate immune response
GO:0002753 cytoplasmic pattern recognition receptor signaling pathway
GO:0006338 chromatin remodeling
GO:0006468 protein phosphorylation
GO:0006954 inflammatory response
GO:0007249 canonical NF-kappaB signal transduction
GO:0009615 response to virus
GO:0010468 regulation of gene expression
GO:0010508 positive regulation of autophagy
GO:0010628 positive regulation of gene expression
GO:0010629 negative regulation of gene expression
GO:0016236 macroautophagy
GO:0016239 positive regulation of macroautophagy
GO:0016310 phosphorylation
GO:0018105 peptidyl-serine phosphorylation
GO:0018107 peptidyl-threonine phosphorylation
GO:0032479 regulation of type I interferon production
GO:0032481 positive regulation of type I interferon production
GO:0032727 positive regulation of interferon-alpha production
GO:0032728 positive regulation of interferon-beta production
GO:0033138 positive regulation of peptidyl-serine phosphorylation
GO:0034142 toll-like receptor 4 signaling pathway
GO:0043123 positive regulation of canonical NF-kappaB signal transduction
GO:0044565 dendritic cell proliferation
GO:0045087 innate immune response
GO:0045944 positive regulation of transcription by RNA polymerase II
GO:0050830 defense response to Gram-positive bacterium
GO:0051607 defense response to virus
GO:0060337 type I interferon-mediated signaling pathway
GO:0060340 positive regulation of type I interferon-mediated signaling pathway
GO:0140374 antiviral innate immune response
GO:0140896 cGAS/STING signaling pathway
GO:1904262 negative regulation of TORC1 signaling
GO:1904263 positive regulation of TORC1 signaling
GO:1904417 positive regulation of xenophagy
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0043231 intracellular membrane-bounded organelle
GO:1902554 serine/threonine protein kinase complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4im3, PDBe:4im3, PDBj:4im3
PDBsum4im3
PubMed23453972
UniProtQ9UHD2|TBK1_HUMAN Serine/threonine-protein kinase TBK1 (Gene Name=TBK1)

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