› 2eu9

X-ray diffraction
1.53Å resolution

Crystal Structure of CLK3

Released:
DOI: 10.2210/pdb2eu9/pdb
PDB entry 2eu9 coloured by chain, front view.
PDB entry 2eu9 coloured by chain, side view.
PDB entry 2eu9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Kinase domain insertions define distinct roles of CLK kinases in SR protein phosphorylation.
Bullock AN, Das S, Debreczeni JE, Rellos P, Fedorov O, Niesen FH, Guo K, Papagrigoriou E, Amos AL, Cho S, Turk BE, Ghosh G, Knapp S
Structure 17 352-62 (2009)
PMID: 19278650

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: 355 amino acids
Theoretical weight: 41.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49761 (Residues: 284-638; Coverage: 56%)
Gene name: CLK3
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2
Unit cell:
a: 108.727Å b: 45.063Å c: 84.006Å
α: 90° β: 115.23° γ: 90°
R-values:
R R work R free
0.171 0.171 0.201
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Phosphorylation mechanism and structure of serine-arginine protein kinases.
Ghosh et al. (2011)
10 more

10 mentions without citation

Substrate and docking interactions in serine/threonine protein kinases.
Goldsmith et al. (2007)
9 more