View source for 3fhx


==Crystal structure of D235A mutant of human pyridoxal kinase==
<StructureSection load='3fhx' size='340' side='right'caption='[[3fhx]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3fhx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FHX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PXL:3-HYDROXY-5-(HYDROXYMETHYL)-2-METHYLISONICOTINALDEHYDE'>PXL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fhx OCA], [https://pdbe.org/3fhx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fhx RCSB], [https://www.ebi.ac.uk/pdbsum/3fhx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fhx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PDXK_HUMAN PDXK_HUMAN] Required for synthesis of pyridoxal-5-phosphate from vitamin B6.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pyridoxal kinase catalyzes the phosphorylation of pyridoxal (PL) to pyridoxal 5'-phosphate (PLP). A D235A variant shows 7-fold and 15-fold decreases in substrate affinity and activity, respectively. A D235N variant shows approximately 2-fold decrease in both PL affinity and activity. The crystal structure of D235A (2.5 A) shows bound ATP, PL and PLP, while D235N (2.3 A) shows bound ATP and sulfate. These results document the role of Asp235 in PL kinase activity. The observation that the active site of PL kinase can accommodate both ATP and PLP suggests that formation of a ternary Enz.PLP.ATP complex could occur in the wild-type enzyme, consistent with severe MgATP substrate inhibition of PL kinase in the presence of PLP.

Kinetic and structural studies of the role of the active site residue Asp235 of human pyridoxal kinase.,Gandhi AK, Ghatge MS, Musayev FN, Sease A, Aboagye SO, di Salvo ML, Schirch V, Safo MK Biochem Biophys Res Commun. 2009 Mar 27;381(1):12-5. Epub 2009 Feb 4. PMID:19351586<ref>PMID:19351586</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3fhx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Pyridoxal kinase|Pyridoxal kinase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Di Salvo ML]]
[[Category: Gandhi AK]]
[[Category: Ghatge M]]
[[Category: Musayev FN]]
[[Category: Safo MK]]
[[Category: Schirch V]]