› 5uvf

X-ray diffraction
2Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189297 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase VRK1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 364 amino acids
Theoretical weight: 41.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99986 (Residues: 3-364; Coverage: 91%)
Gene name: VRK1
Sequence domains: Protein kinase domain
Structure domains: Transferase(Phosphotransferase) domain 1

Ligands and Environments

4 bound ligands:
Ligand 7DZ 4 x 7DZ
Ligand PO4 10 x PO4
Ligand PEG 1 x PEG
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 92.141Å b: 95.242Å c: 192.04Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.204
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Emerging roles of the αC-β4 loop in protein kinase structure, function, evolution, and disease.
Yeung et al. (2020)
1 more

2 mentions without citation

Structural characterization of human Vaccinia-Related Kinases (VRK) bound to small-molecule inhibitors identifies different P-loop conformations.
Couñago et al. (2017)
1 more