3ow1: Difference between revisions

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<StructureSection load='3ow1' size='340' side='right'caption='[[3ow1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3ow1' size='340' side='right'caption='[[3ow1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ow1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_baa-138 Atcc baa-138]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OW1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ow1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Chromohalobacter_salexigens Chromohalobacter salexigens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OW1 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.798&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bsm|3bsm]], [[3p93|3p93]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Csal_2974 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158080 ATCC BAA-138])</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=3ow1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ow1 OCA], [https://pdbe.org/3ow1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ow1 RCSB], [https://www.ebi.ac.uk/pdbsum/3ow1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ow1 ProSAT]</span></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=3ow1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ow1 OCA], [https://pdbe.org/3ow1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ow1 RCSB], [https://www.ebi.ac.uk/pdbsum/3ow1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ow1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DMGD_CHRSD DMGD_CHRSD] Has low dehydratase activity with D-mannonate and D-gluconate, suggesting that these are not physiological substrates and that it has no significant role in the in vivo degradation of these compounds. Has no detectable activity with a panel of 70 other acid sugars (in vitro).<ref>PMID:24697546</ref>


==See Also==
==See Also==
*[[Mandelate racemase/muconate lactonizing enzyme 3D structures|Mandelate racemase/muconate lactonizing enzyme 3D structures]]
*[[Mandelate racemase/muconate lactonizing enzyme 3D structures|Mandelate racemase/muconate lactonizing enzyme 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc baa-138]]
[[Category: Chromohalobacter salexigens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Almo, S C]]
[[Category: Almo SC]]
[[Category: Fedorov, A A]]
[[Category: Fedorov AA]]
[[Category: Fedorov, E V]]
[[Category: Fedorov EV]]
[[Category: Gerlt, J A]]
[[Category: Gerlt JA]]
[[Category: Wichelecki, D]]
[[Category: Wichelecki D]]
[[Category: D-mannonate dehydratase]]
[[Category: Lyase]]

Latest revision as of 12:44, 6 September 2023

Crystal structure of D-mannonate dehydratase from Chromohalobacter salexigens complexed with MGCrystal structure of D-mannonate dehydratase from Chromohalobacter salexigens complexed with MG

Structural highlights

3ow1 is a 8 chain structure with sequence from Chromohalobacter salexigens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.798Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DMGD_CHRSD Has low dehydratase activity with D-mannonate and D-gluconate, suggesting that these are not physiological substrates and that it has no significant role in the in vivo degradation of these compounds. Has no detectable activity with a panel of 70 other acid sugars (in vitro).[1]

See Also

References

  1. Wichelecki DJ, Balthazor BM, Chau AC, Vetting MW, Fedorov AA, Fedorov EV, Lukk T, Patskovsky YV, Stead MB, Hillerich BS, Seidel RD, Almo SC, Gerlt JA. Discovery of function in the enolase superfamily: D-mannonate and d-gluconate dehydratases in the D-mannonate dehydratase subgroup. Biochemistry. 2014 Apr 29;53(16):2722-31. doi: 10.1021/bi500264p. Epub 2014 Apr, 15. PMID:24697546 doi:http://dx.doi.org/10.1021/bi500264p

3ow1, resolution 1.80Å

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