Structure of PDB 4ifc Chain B

Receptor sequence
>4ifcB (length=330) Species: 9606 (Homo sapiens) [Search protein sequence]
DAEGYYRVNIGEVLDKRYNVYGYTGQVFSNVVRARDNARANQEVAVKIIR
NNELMQKTGLKELEFLKKLNDADPDDKFHCLRLFRHFYHKQHLCLVFEPL
SMNLREVLKKYGKDVGLHIKAVRSYSQQLFLALKLLKRCNILHADIKPDN
ILVNESKTILKLCDFGSASHVADNDITPYLVSRFYRAPEIIIGKSYDYGI
DMWSVGCTLYELYTGKILFPGKTNNHMLKLAMDLKGKMPNKMIRKGVFKD
QHFDQNLNFMYIEVDEREKVTVMSTINPTKDLLADLIQRLPEDQRKKVHQ
LKDLLDQILMLDPAKRISINQALQHAFIQE
3D structure
PDB4ifc Evaluation of Cancer Dependence and Druggability of PRP4 Kinase Using Cellular, Biochemical, and Structural Approaches.
ChainB
Resolution2.13 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) D145 K147 N150 D164 S182
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 ADP B T693 V697 F698 S699 V701 A715 K717 E768 L770 L822 D834 T24 V27 F28 S29 V31 A45 K47 E98 L100 L152 D164
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:4ifc, PDBe:4ifc, PDBj:4ifc
PDBsum4ifc
PubMed24003220
UniProtQ13523|PRP4K_HUMAN Serine/threonine-protein kinase PRP4 homolog (Gene Name=PRP4K)

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