4e4f: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e4f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pectobacterium_carotovorum_subsp._carotovorum_PC1 Pectobacterium carotovorum subsp. carotovorum PC1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E4F FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e4f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pectobacterium_carotovorum_subsp._carotovorum_PC1 Pectobacterium carotovorum subsp. carotovorum PC1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E4F FirstGlance]. <br>
</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=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2&#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=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4e4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e4f OCA], [https://pdbe.org/4e4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e4f RCSB], [https://www.ebi.ac.uk/pdbsum/4e4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e4f 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=4e4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e4f OCA], [https://pdbe.org/4e4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e4f RCSB], [https://www.ebi.ac.uk/pdbsum/4e4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e4f ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/MAND_PECCP MAND_PECCP]] Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).<ref>PMID:24697546</ref>  
[https://www.uniprot.org/uniprot/MAND_PECCP MAND_PECCP] Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).<ref>PMID:24697546</ref>  


==See Also==
==See Also==
*[[Enolase 3D structures|Enolase 3D structures]]
*[[Mandelate racemase|Mandelate racemase]]
*[[Mandelate racemase|Mandelate racemase]]
== References ==
== References ==

Latest revision as of 17:52, 14 March 2024

Crystal structure of enolase PC1_0802 (TARGET EFI-502240) from Pectobacterium carotovorum subsp. carotovorum PC1Crystal structure of enolase PC1_0802 (TARGET EFI-502240) from Pectobacterium carotovorum subsp. carotovorum PC1

Structural highlights

4e4f is a 4 chain structure with sequence from Pectobacterium carotovorum subsp. carotovorum PC1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MAND_PECCP Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. 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

4e4f, resolution 2.00Å

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