› 6fyp

X-ray diffraction
2.29Å resolution

X-RAY STRUCTURE OF CLK3-KD(GP-[275-632], NON-PHOS.)/CX-4945 AT 2.29A

Released:
DOI: 10.2210/pdb6fyp/pdb
Model geometry
Fit model/data
PDB entry 6fyp coloured by chain, front view.
PDB entry 6fyp coloured by chain, side view.
PDB entry 6fyp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
X-ray Structures and Feasibility Assessment of CLK2 Inhibitors for Phelan-McDermid Syndrome.
Kallen J, Bergsdorf C, Arnaud B, Bernhard M, Brichet M, Cobos-Correa A, Elhajouji A, Freuler F, Galimberti I, Guibourdenche C, Haenni S, Holzinger S, Hunziker J, Izaac A, Kaufmann M, Leder L, Martus HJ, von Matt P, Polyakov V, Roethlisberger P, Roma G, Stiefl N, Uteng M, Lerchner A
ChemMedChem 13 1997-2007 (2018)
PMID: 29985556

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-156013 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein kinase CLK3 Chain: A
Molecule details ›
Chain: A
Length: 360 amino acids
Theoretical weight: 42.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P49761 (Residues: 127-484; Coverage: 73%)
Gene name: CLK3
Sequence domains: Protein kinase domain
Structure domains: Phosphorylase Kinase; domain 1

Ligands and Environments

1 bound ligand:
Ligand 3NG 1 x 3NG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2
Unit cell:
a: 91.197Å b: 61.998Å c: 73.328Å
α: 90° β: 97.1° γ: 90°
R-values:
R R work R free
0.23 0.228 0.267
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Cdc-Like Kinases (CLKs): Biology, Chemical Probes, and Therapeutic Potential.
Martín Moyano et al. (2020)
2 more

1 mention without citation

Dual-Specificity, Tyrosine Phosphorylation-Regulated Kinases (DYRKs) and cdc2-Like Kinases (CLKs) in Human Disease, an Overview.
Lindberg et al. (2021)