Structure of PDB 4ijp Chain A

Receptor sequence
>4ijpA (length=331) Species: 9606 (Homo sapiens) [Search protein sequence]
DAEGYYRVNIGEVLDKRYNVYGYTGQGVFSNVVRARDNARANQEVAVKII
RNNELMQKTGLKELEFLKKLNDADPDDKFHCLRLFRHFYHKQHLCLVFEP
LSMNLREVLKKYGKDVGLHIKAVRSYSQQLFLALKLLKRCNILHADIKPD
NILVNESKTILKLCDFGSASHVADNDITPYLVSRFYRAPEIIIGKSYDYG
IDMWSVGCTLYELYTGKILFPGKTNNHMLKLAMDLKGKMPNKMIRKGVFK
DQHFDQNLNFMYIEVDEREKVTVMSTINPTKDLLADLIQRLPEDQRKKVH
QLKDLLDQILMLDPAKRISINQALQHAFIQE
3D structure
PDB4ijp Evaluation of Cancer Dependence and Druggability of PRP4 Kinase Using Cellular, Biochemical, and Structural Approaches.
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D815 K817 N820 D834 S852
Catalytic site (residue number reindexed from 1) D146 K148 N151 D165 S183
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 A T693 V701 A715 K717 L751 F767 L770 S771 M772 E776 L822 T24 V32 A46 K48 L82 F98 L101 S102 M103 E107 L153 MOAD: ic50=0.016uM
PDBbind-CN: -logKd/Ki=7.80,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

View graph for
Molecular Function
View graph for
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)

[Back to BioLiP]