› 2xkd

X-ray diffraction
1.96Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156438 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase Nek2 Chain: A
Molecule details ›
Chain: A
Length: 279 amino acids
Theoretical weight: 32.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P51955 (Residues: 1-271; Coverage: 61%)
Gene names: NEK2, NEK2A, NLK1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand T3M 1 x T3M
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: C2
Unit cell:
a: 100.28Å b: 57.06Å c: 73.76Å
α: 90° β: 127.61° γ: 90°
R-values:
R R work R free
0.183 0.181 0.217
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Cell cycle regulation by the NEK family of protein kinases.
Fry et al. (2012)
10 more

2 mentions without citation

Aminopyrazine inhibitors binding to an unusual inactive conformation of the mitotic kinase Nek2: SAR and structural characterization.
Whelligan et al. (2010)
1 more