PDBe 2pup

X-ray diffraction
2.6Å resolution

Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding

Released:

Function and Biology Details

Reaction catalysed:
ATP + S-methyl-5-thio-D-ribose = ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate. 
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methylthioribose kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 397 amino acids
Theoretical weight: 45.14 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O31663 (Residues: 1-397; Coverage: 100%)
Gene names: BSU13560, mtnK, ykrT
Sequence domains: Phosphotransferase enzyme family
Structure domains: Phosphorylase Kinase; domain 1

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21212
Unit cell:
a: 213.93Å b: 83.29Å c: 51.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.211 0.274
Expression system: Escherichia coli BL21