› 5unp

X-ray diffraction
2.92Å resolution

Structure of CDC2-Like Kinase 2 (CLK2) in Complex with Compound T-025 [N2-methyl-N4-(pyrimidin-2-ylmethyl)-5-(quinolin-6-yl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine]

Released:
DOI: 10.2210/pdb5unp/pdb
PDB entry 5unp coloured by chain, front view.
PDB entry 5unp coloured by chain, side view.
PDB entry 5unp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A novel CLK inhibitor exhibits anti-tumor efficacies via modulating pre-mRNA splicing and targeting a MYC-dependent vulnerability
Iwai K, Yaguchi M, Klein MG
EMBO Mol Med (2018)

Function and Biology Details

Reaction catalysed: 
ATP + L-seryl/L-threonyl/L-tyrosyl-[protein] = ADP + O-phospho-L-seryl/O-phospho-L-threonyl/O-phospho-L-tyrosyl-[protein]
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156011 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein kinase CLK2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 369 amino acids
Theoretical weight: 43.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: P49760 (Residues: 129-496; Coverage: 74%)
Gene name: CLK2
Sequence domains: Protein kinase domain
Structure domains: Phosphorylase Kinase; domain 1

Ligands and Environments

1 bound ligand:
Ligand 8FY 2 x 8FY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: I41
Unit cell:
a: 141.252Å b: 141.252Å c: 124.37Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.201 0.234
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

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