Structure of PDB 5j79 Chain A

Receptor sequence
>5j79A (length=283) Species: 9606 (Homo sapiens) [Search protein sequence]
NGEAICSALPTIPYHKLADLRYLSRGASGTVSSARHADWRVQVAVKHLRK
DVLREAEILHKARFSYILPILGICNEPEFLGIVTEYMPNGSLNELLHRKT
EYPDVAWPLRFRILHEIALGVNYLHNMTPPLLHHDLKTQNILLDNEFHVK
IADFGLSKWRMSAPEGGTIIYMPPENYEPSIKHDIYSYAVITWEVLSRKQ
PFEDVTNPLQIMYSVSQGHRPVINEESLPYDIPHRARMISLIESGWAQNP
DERPSFLKCLIELEPVLRTFEEITFLEAVIQLK
3D structure
PDB5j79 The Identification and Pharmacological Characterization of 6-(tert-Butylsulfonyl)-N-(5-fluoro-1H-indazol-3-yl)quinolin-4-amine (GSK583), a Highly Potent and Selective Inhibitor of RIP2 Kinase.
ChainA
Resolution2.69 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D146 K148 Q150 N151 D164 P185 T189
Catalytic site (residue number reindexed from 1) D135 K137 Q139 N140 D153 P164 T168
Enzyme Commision number 2.7.10.2: non-specific protein-tyrosine kinase.
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 6GE A S25 A45 K47 E66 L79 T95 M98 L153 D164 S24 A44 K46 E55 L68 T84 M87 L142 D153 PDBbind-CN: -logKd/Ki=8.52,IC50=3nM
BindingDB: IC50=20nM
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:5j79, PDBe:5j79, PDBj:5j79
PDBsum5j79
PubMed27109867
UniProtO43353|RIPK2_HUMAN Receptor-interacting serine/threonine-protein kinase 2 (Gene Name=RIPK2)

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