› 3op5

X-ray diffraction
2.4Å 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 BL21(DE3)
UniProt:
  • Canonical: Q99986 (Residues: 3-364; Coverage: 91%)
Gene name: VRK1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand REB 4 x REB
Ligand EDO 5 x EDO
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 92.97Å b: 97.19Å c: 191.99Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.178 0.213
Expression system: Escherichia coli BL21(DE3)

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

10 mentions without citation

The "Sticky Patch" Model of Crystallization and Modification of Proteins for Enhanced Crystallizability.
Derewenda et al. (2017)
9 more