3sbf: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='3sbf' size='340' side='right'caption='[[3sbf]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='3sbf' size='340' side='right'caption='[[3sbf]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3sbf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibbs Vibbs]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SBF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SBF FirstGlance]. <br>
<table><tr><td colspan='2'>[[3sbf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrionales_bacterium_SWAT-3 Vibrionales bacterium SWAT-3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SBF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SBF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D8T:D-ARABINONIC+ACID'>D8T</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</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]] 1.5&#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;'>[[3r25|3r25]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D8T:D-ARABINONIC+ACID'>D8T</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VSWAT3_13707 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=391574 VIBBS])</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=3sbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sbf OCA], [https://pdbe.org/3sbf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sbf RCSB], [https://www.ebi.ac.uk/pdbsum/3sbf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sbf 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=3sbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sbf OCA], [https://pdbe.org/3sbf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sbf RCSB], [https://www.ebi.ac.uk/pdbsum/3sbf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sbf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/IMAND_VIBBS IMAND_VIBBS]] Has no detectable activity with D-mannonate and with a panel of 70 other acid sugars (in vitro), in spite of the conservation of the residues that are expected to be important for catalytic activity and cofactor binding. May have evolved a divergent function.<ref>PMID:24697546</ref>
[https://www.uniprot.org/uniprot/IMAND_VIBBS IMAND_VIBBS] Has no detectable activity with D-mannonate and with a panel of 70 other acid sugars (in vitro), in spite of the conservation of the residues that are expected to be important for catalytic activity and cofactor binding. May have evolved a divergent function.<ref>PMID:24697546</ref>  


==See Also==
==See Also==
*[[Enolase 3D structures|Enolase 3D structures]]
*[[Mandelate racemase|Mandelate racemase]]
*[[Mandelate racemase|Mandelate racemase]]
*[[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]]
Line 20: Line 20:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Vibbs]]
[[Category: Vibrionales bacterium SWAT-3]]
[[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: Acid sugar dehydratase]]
[[Category: D-araninonate]]
[[Category: Enolase fold]]
[[Category: Isomerase]]

Latest revision as of 15:52, 14 March 2024

Crystal structure of the mutant P311A of enolase superfamily member from VIBRIONALES BACTERIUM complexed with Mg and D-ArabinonateCrystal structure of the mutant P311A of enolase superfamily member from VIBRIONALES BACTERIUM complexed with Mg and D-Arabinonate

Structural highlights

3sbf is a 4 chain structure with sequence from Vibrionales bacterium SWAT-3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IMAND_VIBBS Has no detectable activity with D-mannonate and with a panel of 70 other acid sugars (in vitro), in spite of the conservation of the residues that are expected to be important for catalytic activity and cofactor binding. May have evolved a divergent function.[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

3sbf, resolution 1.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA