3qdk

X-ray diffraction
2.31Å resolution

Structural insight on mechanism and diverse substrate selection strategy of ribulokinase

Released:

Function and Biology Details

Reaction catalysed:
ATP + L(or D)-ribulose = ADP + L(or D)-ribulose 5-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribulokinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 572 amino acids
Theoretical weight: 62.85 KDa
Source organism: Bacillus halodurans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9KBQ3 (Residues: 3-563; Coverage: 100%)
Gene names: BH1872, araB
Sequence domains:
Structure domains: Nucleotidyltransferase; domain 5

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C, NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 56.683Å b: 88.84Å c: 230.525Å
α: 90° β: 92.75° γ: 90°
R-values:
R R work R free
0.224 0.224 0.274
Expression system: Escherichia coli BL21(DE3)