Pyridoxal kinase
From Proteopedia
(Difference between revisions)
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*'''Pyridoxal kinase''' | *'''Pyridoxal kinase''' | ||
- | **[[1lhp]] – sPDX – sheep<br /> | ||
**[[2f7k]] – hPDX - human<br /> | **[[2f7k]] – hPDX - human<br /> | ||
+ | **[[1lhp]] – sPDX – sheep<br /> | ||
**[[2ddm]] – EcPDX1 – ''Escherichia coli''<br /> | **[[2ddm]] – EcPDX1 – ''Escherichia coli''<br /> | ||
**[[3h74]] – LpPDX – ''Lactobacillus planarum'' <br /> | **[[3h74]] – LpPDX – ''Lactobacillus planarum'' <br /> | ||
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**[[5trw]] - PDX - ''Burkholderia xenovorans''<br /> | **[[5trw]] - PDX - ''Burkholderia xenovorans''<br /> | ||
**[[5b6a]] - PDX - ''Pseudomonas aeruginosa''<br /> | **[[5b6a]] - PDX - ''Pseudomonas aeruginosa''<br /> | ||
+ | **[[5zw9]] – PDX – ''Salmonella choleraesuis''<br /> | ||
*Pyridoxal kinase complex with pyridoxal compounds | *Pyridoxal kinase complex with pyridoxal compounds | ||
+ | **[[3fhx]] – hPDX (mutant) + Mg + Na + ATP + pyridoxal + pyridoxal-5’-phosphate <br /> | ||
+ | **[[3keu]] – hPDX + Mg + ATP + pyridoxal-5’-phosphate<br /> | ||
**[[1rft]] – sPDX + Zn + K + AMPPCP + pyridoxamine<br /> | **[[1rft]] – sPDX + Zn + K + AMPPCP + pyridoxamine<br /> | ||
**[[1rfu]] – sPDX + Zn + ADP + pyridoxal-5’-phosphate<br /> | **[[1rfu]] – sPDX + Zn + ADP + pyridoxal-5’-phosphate<br /> | ||
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**[[4c5l]] – SaPDX + pyridoxal<br /> | **[[4c5l]] – SaPDX + pyridoxal<br /> | ||
**[[4c5n]] – SaPDX + pyridoxal + AMPPCP<br /> | **[[4c5n]] – SaPDX + pyridoxal + AMPPCP<br /> | ||
- | **[[3fhx]] – hPDX (mutant) + Mg + Na + ATP + pyridoxal + pyridoxal-5’-phosphate <br /> | ||
- | **[[3keu]] – hPDX + Mg + ATP + pyridoxal-5’-phosphate<br /> | ||
**[[4s1i]] – EhPDX + Mg + pyridoxal-5’-phosphate - ''Entamoeba histolytica'' <br /> | **[[4s1i]] – EhPDX + Mg + pyridoxal-5’-phosphate - ''Entamoeba histolytica'' <br /> | ||
+ | **[[6su9]] – PDX + pyridoxal + AMPPNP – ''Plasmodium falciparum''<br /> | ||
*Other pyridoxal kinase complexes | *Other pyridoxal kinase complexes | ||
+ | **[[2ajp]] – hPDX + Mg + ANP <br /> | ||
+ | **[[2yxt]] – hPDX + Na + Pi<br /> | ||
+ | **[[2yxu]] – hPDX + Mg + Na + ATP + Pi<br /> | ||
+ | **[[3fhy]] – hPDX (mutant) + Mg + Na + ATP <br /> | ||
+ | **[[4en4]] – hPDX + Mg + ATP + ginkotoxin<br /> | ||
+ | **[[4eoh]] – hPDX + Na + theophylline<br /> | ||
**[[1lhr]] – sPDX + Zn + K + ATP<br /> | **[[1lhr]] – sPDX + Zn + K + ATP<br /> | ||
**[[1rfv]] – sPDX + Zn + ADP <br /> | **[[1rfv]] – sPDX + Zn + ADP <br /> | ||
**[[1ygj]], [[1ygk]], [[1yhj]] – sPDX + roscovitine<br /> | **[[1ygj]], [[1ygk]], [[1yhj]] – sPDX + roscovitine<br /> | ||
- | **[[2ajp]] – hPDX + Mg + ANP <br /> | ||
**[[2ddo]] – EcPDX1 + Mg + ATP + Pi<br /> | **[[2ddo]] – EcPDX1 + Mg + ATP + Pi<br /> | ||
**[[2i5b]] – PDX + ADP – ''Bacillus subtilis''<br /> | **[[2i5b]] – PDX + ADP – ''Bacillus subtilis''<br /> | ||
- | **[[2yxt]] – hPDX + Na + Pi<br /> | ||
- | **[[2yxu]] – hPDX + Mg + Na + ATP + Pi<br /> | ||
- | **[[3fhy]] – hPDX (mutant) + Mg + Na + ATP <br /> | ||
**[[3hyo]] – LpPDX + Mg + ADP <br /> | **[[3hyo]] – LpPDX + Mg + ADP <br /> | ||
**[[3ibq]] – LpPDX + Mg + ATP <br /> | **[[3ibq]] – LpPDX + Mg + ATP <br /> | ||
- | **[[4en4]] – hPDX + Mg + ATP + ginkotoxin<br /> | ||
- | **[[4eoh]] – hPDX + Na + theophylline<br /> | ||
**[[4c5k]] – SaPDX + ADP<br /> | **[[4c5k]] – SaPDX + ADP<br /> | ||
**[[4c5m]] – SaPDX + AMPPCP<br /> | **[[4c5m]] – SaPDX + AMPPCP<br /> |
Revision as of 10:44, 5 December 2019
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3D Structures of pyridoxal kinase
Updated on 05-December-2019
References
- ↑ di Salvo ML, Nogues I, Parroni A, Tramonti A, Milano T, Pascarella S, Contestabile R. On the mechanism of Escherichia coli pyridoxal kinase inhibition by pyridoxal and pyridoxal 5'-phosphate. Biochim Biophys Acta. 2015 Sep;1854(9):1160-6. doi: 10.1016/j.bbapap.2015.01.013., Epub 2015 Feb 3. PMID:25655354 doi:http://dx.doi.org/10.1016/j.bbapap.2015.01.013
- ↑ Safo MK, Musayev FN, di Salvo ML, Hunt S, Claude JB, Schirch V. Crystal structure of pyridoxal kinase from the Escherichia coli pdxK gene: implications for the classification of pyridoxal kinases. J Bacteriol. 2006 Jun;188(12):4542-52. PMID:16740960 doi:188/12/4542