› 6oid

X-ray diffraction
2.36Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + [protein]-N(6)-D-ribulosyl-L-lysine = ADP + [protein]-N(6)-(3-O-phospho-D-ribulosyl)-L-lysine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192269 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-ribulosamine 3-kinase, chloroplastic Chains: A, B
Molecule details ›
Chains: A, B
Length: 317 amino acids
Theoretical weight: 35.47 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9LEW8 (Residues: 30-326; Coverage: 91%)
Gene names: At3g61080, T27I15_170
Sequence domains: Fructosamine kinase

Ligands and Environments

5 bound ligands:
Ligand ADP 2 x ADP
Ligand SO4 14 x SO4
Ligand CL 2 x CL
Ligand EDO 5 x EDO
Ligand DMS 2 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2221
Unit cell:
a: 158.86Å b: 163.64Å c: 70.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.175 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

The Taming of Nuclear Factor Erythroid-2-Related Factor-2 (Nrf2) Deglycation by Fructosamine-3-Kinase (FN3K)-Inhibitors-A Novel Strategy to Combat Cancers.
Beeraka et al. (2021)
3 more

2 mentions without citation

Activation mechanism of PINK1.
Gan et al. (2022)
1 more