Structure of PDB 4eut Chain A

Receptor sequence
>4eutA (length=384) Species: 9606 (Homo sapiens) [Search protein sequence]
GSQSTSNHLWLLSDILGQGATANVFRGRHKKTGDLFAIKVFNNISFLRPV
DVQMREFEVLKKLNHKNIVKLFAIEEETTTRHKVLIMEFCPCGSLYTVLE
EPSNAYGLPESEFLIVLRDVVGGMNHLRENGIVHRNIKPGNIMRVIGEDG
QSVYKLTDFGAARELEDDEQFVSLYGTEEYLHPDMYERAVLDHQKKYGAT
VDLWSIGVTFYHAATGSLPFRPFEGPRRNKEVMYKIITGKPSGAISGVQK
AENGPIDWSGDMPVSCSLSRGLQVLLTPVLANILEADQEKCWGFDQFFAE
TSDILHRMVIHVFSLQQMTAHKIYIHSYNTATIFHELVYKQTKIISSNQE
LIYEGRRLVLEPGRLAQHFPKTTEENPIFVVSRE
3D structure
PDB4eut Molecular basis of Tank-binding kinase 1 activation by transautophosphorylation.
ChainA
Resolution2.6 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 T176
Catalytic site (residue number reindexed from 1) N136 K138 N141 D158 T177
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 L15 G16 Q17 G18 V23 A36 M86 E87 C89 P90 G92 M142 D157 L16 G17 Q18 G19 V24 A37 M87 E88 C90 P91 G93 M143 D158 BindingDB: IC50=8.0nM,Kd=158nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:4eut, PDBe:4eut, PDBj:4eut
PDBsum4eut
PubMed22619329
UniProtQ9UHD2|TBK1_HUMAN Serine/threonine-protein kinase TBK1 (Gene Name=TBK1)

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