3thu: Difference between revisions

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New page: '''Unreleased structure''' The entry 3thu is ON HOLD Authors: Vetting, M.W., Toro, R., Bhosle, R., Wasserman, S.R., Morisco, L.L., Hillerich, B., Washington, E., Scott Glen, A., Chowhur...
 
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'''Unreleased structure'''


The entry 3thu is ON HOLD
==Crystal structure of an enolase from sphingomonas sp. ska58 (efi target efi-501683) with bound mg==
<StructureSection load='3thu' size='340' side='right'caption='[[3thu]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3thu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_sp._SKA58 Sphingomonas sp. SKA58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3THU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3THU 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]] 1.8&#8491;</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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=3thu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thu OCA], [https://pdbe.org/3thu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3thu RCSB], [https://www.ebi.ac.uk/pdbsum/3thu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3thu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MAND_SPHSS MAND_SPHSS] Catalyzes the dehydration of D-mannonate. Has no detectable activity with a panel of 70 other acid sugars (in vitro).<ref>PMID:24697546</ref>


Authors: Vetting, M.W., Toro, R., Bhosle, R., Wasserman, S.R., Morisco, L.L., Hillerich, B., Washington, E., Scott Glen, A., Chowhurdy, S., Evans, B., Hammond, J., Zencheck, W.D., Imker, H.J., Gerlt, J.A., Almo, S.C., Enzyme Function Initiative (EFI)
==See Also==
 
*[[Enolase 3D structures|Enolase 3D structures]]
Description: Crystal structure of an enolase from sphingomonas sp. ska58 (efi target efi-501683) with bound mg
*[[Mandelate racemase|Mandelate racemase]]
*[[Mandelate racemase/muconate lactonizing enzyme 3D structures|Mandelate racemase/muconate lactonizing enzyme 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sphingomonas sp. SKA58]]
[[Category: Almo SC]]
[[Category: Bhosle R]]
[[Category: Chowdhury S]]
[[Category: Evans B]]
[[Category: Gerlt JA]]
[[Category: Hammonds J]]
[[Category: Hillerich B]]
[[Category: Imker HJ]]
[[Category: Morisco LL]]
[[Category: Scott Glenn A]]
[[Category: Toro R]]
[[Category: Vetting MW]]
[[Category: Washington E]]
[[Category: Wasserman SR]]
[[Category: Zencheck WD]]

Latest revision as of 16:29, 14 March 2024

Crystal structure of an enolase from sphingomonas sp. ska58 (efi target efi-501683) with bound mgCrystal structure of an enolase from sphingomonas sp. ska58 (efi target efi-501683) with bound mg

Structural highlights

3thu is a 3 chain structure with sequence from Sphingomonas sp. SKA58. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MAND_SPHSS Catalyzes the dehydration of D-mannonate. 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

3thu, resolution 1.80Å

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