Structure of PDB 4ijp Chain B

Receptor sequence
>4ijpB (length=334) Species: 9606 (Homo sapiens) [Search protein sequence]
WTDAEGYYRVNIGEVLDKRYNVYGYTGQGVFSNVVRARDNARANQEVAVK
IIRNNELMQKTGLKELEFLKKLNDADPDDKFHCLRLFRHFYHKQHLCLVF
EPLSMNLREVLKKYGKDVGLHIKAVRSYSQQLFLALKLLKRCNILHADIK
PDNILVNESKTILKLCDFGSASHVADNDITPYLVSRFYRAPEIIIGKSYD
YGIDMWSVGCTLYELYTGKILFPGKTNNHMLKLAMDLKGKMPNKMIRKGV
FKDQHFDQNLNFMYIEVDREKVTVMSTINPTKDLLADLIGCQRLPEDQRK
KVHQLKDLLDQILMLDPAKRISINQALQHAFIQE
3D structure
PDB4ijp Evaluation of Cancer Dependence and Druggability of PRP4 Kinase Using Cellular, Biochemical, and Structural Approaches.
ChainB
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D815 K817 N820 D834 S852
Catalytic site (residue number reindexed from 1) D148 K150 N153 D167 S185
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 1EH B T693 V701 R703 K717 L751 L770 S771 M772 E776 L822 T26 V34 R36 K50 L84 L103 S104 M105 E109 L155 MOAD: ic50=0.016uM
BindingDB: IC50=16nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation
GO:0045292 mRNA cis splicing, via spliceosome

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Molecular Function
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Biological Process
External links
PDB RCSB:4ijp, PDBe:4ijp, PDBj:4ijp
PDBsum4ijp
PubMed24003220
UniProtQ13523|PRP4K_HUMAN Serine/threonine-protein kinase PRP4 homolog (Gene Name=PRP4K)

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