3bsm: Difference between revisions

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==Crystal structure of D-mannonate dehydratase from Chromohalobacter salexigens==
==Crystal structure of D-mannonate dehydratase from Chromohalobacter salexigens==
<StructureSection load='3bsm' size='340' side='right'caption='[[3bsm]]' scene=''>
<StructureSection load='3bsm' size='340' side='right'caption='[[3bsm]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BSM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BSM FirstGlance]. <br>
<table><tr><td colspan='2'>[[3bsm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chromohalobacter_salexigens_DSM_3043 Chromohalobacter salexigens DSM 3043]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BSM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BSM FirstGlance]. <br>
</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=3bsm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bsm OCA], [https://pdbe.org/3bsm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bsm RCSB], [https://www.ebi.ac.uk/pdbsum/3bsm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bsm ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/3bsm TOPSAN]</span></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]] 2.2&#8491;</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=3bsm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bsm OCA], [https://pdbe.org/3bsm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bsm RCSB], [https://www.ebi.ac.uk/pdbsum/3bsm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bsm ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/3bsm TOPSAN]</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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==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: Chromohalobacter salexigens DSM 3043]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Almo SC]]
[[Category: Almo SC]]

Latest revision as of 12:31, 21 February 2024

Crystal structure of D-mannonate dehydratase from Chromohalobacter salexigensCrystal structure of D-mannonate dehydratase from Chromohalobacter salexigens

Structural highlights

3bsm is a 4 chain structure with sequence from Chromohalobacter salexigens DSM 3043. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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

3bsm, resolution 2.20Å

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