4fi4: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4fi4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_sp._K31 Caulobacter sp. K31]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FI4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4fi4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_sp._K31 Caulobacter sp. K31]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FI4 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</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=4fi4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fi4 OCA], [https://pdbe.org/4fi4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fi4 RCSB], [https://www.ebi.ac.uk/pdbsum/4fi4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fi4 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=4fi4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fi4 OCA], [https://pdbe.org/4fi4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fi4 RCSB], [https://www.ebi.ac.uk/pdbsum/4fi4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fi4 ProSAT]</span></td></tr>
</table>
</table>

Latest revision as of 18:25, 14 March 2024

Crystal structure of mannonate dehydratase PRK15072 (TARGET EFI-502214) from Caulobacter sp. K31Crystal structure of mannonate dehydratase PRK15072 (TARGET EFI-502214) from Caulobacter sp. K31

Structural highlights

4fi4 is a 3 chain structure with sequence from Caulobacter sp. K31. 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

MAND1_CAUSK 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

4fi4, resolution 2.00Å

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