2pu8 Summary

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

The structure was published by Ku, S.-Y., Yip, P., Cornell, K.A., et al., Behr, J.-B., Guillerm, G., and Howell, P.L., in 2007 in a paper entitled "Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2007.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Methylthioribose kinase.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Methylthioribose kinase O31663 (1-397) (MTNK_BACSU)search Bacillus subtilis subsp. subtilis str. 168search 100% 397 93%
B Methylthioribose kinase O31663 (1-397) (MTNK_BACSU)search Bacillus subtilis subsp. subtilis str. 168search 100% 397 93%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
O31663 (1 - 397) Methylthioribose kinase Bacillus subtilis

Chain Structural classification (SCOP) Sequence family (Pfam)
A, B (O31663) APH phosphotransferasessearch PF01636: Phosphotransferase enzyme familysearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (O31663) nucleotide bindingsearch ATP bindingsearch kinase activitysearch transferase activitysearch transferase activity, transferring phosphorus-containing groupssearch S-methyl-5-thioribose kinase activitysearch response to stresssearch cellular amino acid biosynthetic processsearch methionine biosynthetic processsearch phosphorylationsearch L-methionine biosynthetic process from S-adenosylmethioninesearch L-methionine biosynthetic process from methylthioadenosinesearch

Chain InterPro annotation
A, B Aminoglycoside phosphotransferasesearch Methylthioribose kinasesearch Protein kinase-like domainsearch