Structure of PDB 6cnh Chain A

Receptor sequence
>6cnhA (length=321) Species: 9606 (Homo sapiens) [Search protein sequence]
SMDFWTDAEGYYRVNIGEVLDKRYNVYGYTGQGVFSNVVRARDNARANQE
VAVKIIRNNELMQKTGLKELEFLKKLNDADPDDKFHCLRLLRHFYHKQHL
CLVFEPLSMNLREVLKKYGKDVGLHIKAVRSYSQQLFLALKLLKRCNILH
ADIKPDNILVNESKTILKLCDFLFSRFYRAPEIIIGKSYDYGIDMWSVGC
TLYELYTGKILFPGKTNNHMLKLAMDLKGKMPNKMIRKGVFKDQHFDQNL
NFMYIEEKVTVMSTINPTKDLLADLIGCQRLPEDQRKKVHQLKDLLDQIL
MLDPAKRISINQALQHAFIQE
3D structure
PDB6cnh Crystal structure of the human PRPF4B in complex with Rebastinib
ChainA
Resolution2.0 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) D152 K154 N157 D171 S175
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 919 A S655 T693 Q695 V701 R703 A715 K717 T728 E732 L739 L751 F767 L770 C833 D834 F835 S1 T30 Q32 V38 R40 A52 K54 T65 E69 L76 L88 F104 L107 C170 D171 F172
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

View graph for
Biological Process
External links
PDB RCSB:6cnh, PDBe:6cnh, PDBj:6cnh
PDBsum6cnh
PubMed
UniProtQ13523|PRP4K_HUMAN Serine/threonine-protein kinase PRP4 homolog (Gene Name=PRP4K)

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