› 2lav

Solution NMR

NMR solution structure of human Vaccinia-Related Kinase 1

Released:
DOI: 10.2210/pdb2lav/pdb
PDB entry 2lav coloured by chain, ensemble of 20 models, front view.
PDB entry 2lav coloured by chain, ensemble of 20 models, side view.
PDB entry 2lav coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
NMR solution structure of human vaccinia-related kinase 1 (VRK1) reveals the C-terminal tail essential for its structural stability and autocatalytic activity.
Shin J, Chakraborty G, Bharatham N, Kang C, Tochio N, Koshiba S, Kigawa T, Kim W, Kim KT, Yoon HS
J Biol Chem 286 22131-8 (2011)
PMID: 21543316

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 Chain: A
Molecule details ›
Chain: A
Length: 361 amino acids
Theoretical weight: 41.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99986 (Residues: 1-361; Coverage: 91%)
Gene name: VRK1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 73%
Refinement method: simulated annealing
Expression system: Escherichia coli

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Citations

3 review citations

Plant innate immunity: perception of conserved microbial signatures.
Schwessinger et al. (2012)
2 more

9 mentions without citation

NMR solution structure of human vaccinia-related kinase 1 (VRK1) reveals the C-terminal tail essential for its structural stability and autocatalytic activity.
Shin et al. (2011)
8 more