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==Crystal structure of Triosephosphate isomerase from Stenotrophomonas maltophilia K279a== | |||
<StructureSection load='6w4u' size='340' side='right'caption='[[6w4u]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6w4u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia_K279a Stenotrophomonas maltophilia K279a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6W4U 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]] 1.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=6w4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w4u OCA], [https://pdbe.org/6w4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6w4u RCSB], [https://www.ebi.ac.uk/pdbsum/6w4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6w4u ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TPIS_STRMK TPIS_STRMK] Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | |||
==See Also== | |||
*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]] | |||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Stenotrophomonas maltophilia K279a]] |
Latest revision as of 17:16, 18 October 2023
Crystal structure of Triosephosphate isomerase from Stenotrophomonas maltophilia K279aCrystal structure of Triosephosphate isomerase from Stenotrophomonas maltophilia K279a
Structural highlights
FunctionTPIS_STRMK Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). See Also |
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