Structure of PDB 5ar7 Chain B

Receptor sequence
>5ar7B (length=278) Species: 9606 (Homo sapiens) [Search protein sequence]
ICSALPTIPYHKLADLRYLSRGASGTVSSARHADWRVQVAVKHLHLDSER
KDVLREAEILHKARFSYILPILGICNEPEFLGIVTEYMPNGSLNELLHRK
TEYPDVAWPLRFRILHEIALGVNYLHNMTPPLLHHDLKTQNILLDNEFHV
KIADFGGTIIYMPPENYEPGQKSRASIKHDIYSYAVITWEVLSRKQPFED
VTNPLQIMYSVSQGRPVINEESLPYDIPHRARMISLIESGWAQNPDERPS
FLKCLIELEPVLRTFEEITFLEAVIQLK
3D structure
PDB5ar7 Crystal Structures of Human Rip2 Kinase Catalytic Domain Complexed with ATP-Competitive Inhibitors: Foundations for Understanding Inhibitor Selectivity.
ChainB
Resolution2.71 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 T189
Catalytic site (residue number reindexed from 1) D136 K138 Q140 N141 D154 T158
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 SR8 B A45 E66 L70 L79 M98 L153 I162 A163 D164 F165 A40 E56 L60 L69 M88 L143 I152 A153 D154 F155 BindingDB: IC50=320nM
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:5ar7, PDBe:5ar7, PDBj:5ar7
PDBsum5ar7
PubMed26455654
UniProtO43353|RIPK2_HUMAN Receptor-interacting serine/threonine-protein kinase 2 (Gene Name=RIPK2)

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