6csw

X-ray diffraction
2.25Å resolution

Crystal Structure of the Human vaccinia-related kinase bound to a N-methyl-N-propyl-dihydropteridine inhibitor

Released:
Source organism: Homo sapiens
Entry authors: dos Reis CV, de Souza GP, Counago RM, Chiodi CG, Azevedo A, Guimaraes C, Mascarello A, Gama F, Ferreira M, Massirer KB, Arruda P, Edwards AM, Elkins JM, Structural Genomics Consortium (SGC)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (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: Transferase(Phosphotransferase) domain 1

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P212121
Unit cell:
a: 91.83Å b: 96.987Å c: 191.67Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.188 0.233
Expression system: Escherichia coli BL21(DE3)