1v71: Difference between revisions

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==Crystal Structure of S.pombe Serine Racemase==
==Crystal Structure of S.pombe Serine Racemase==
<StructureSection load='1v71' size='340' side='right' caption='[[1v71]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1v71' size='340' side='right'caption='[[1v71]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1v71]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V71 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V71 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1v71]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V71 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 1.7&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v71 OCA], [http://pdbe.org/1v71 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v71 RCSB], [http://www.ebi.ac.uk/pdbsum/1v71 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v71 ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=1v71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v71 OCA], [https://pdbe.org/1v71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v71 RCSB], [https://www.ebi.ac.uk/pdbsum/1v71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v71 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SRR_SCHPO SRR_SCHPO]] Catalyzes the synthesis of D-serine from L-serine. Has dehydratase activity towards both L-serine and D-serine.<ref>PMID:19640845</ref>
[https://www.uniprot.org/uniprot/SRR_SCHPO SRR_SCHPO] Catalyzes the synthesis of D-serine from L-serine. Has dehydratase activity towards both L-serine and D-serine.<ref>PMID:19640845</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cbs 356]]
[[Category: Large Structures]]
[[Category: Goto, M]]
[[Category: Schizosaccharomyces pombe]]
[[Category: Dimer]]
[[Category: Goto M]]
[[Category: Isomerase]]
[[Category: Plp]]

Latest revision as of 02:58, 28 December 2023

Crystal Structure of S.pombe Serine RacemaseCrystal Structure of S.pombe Serine Racemase

Structural highlights

1v71 is a 1 chain structure with sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SRR_SCHPO Catalyzes the synthesis of D-serine from L-serine. Has dehydratase activity towards both L-serine and D-serine.[1]

Evolutionary Conservation

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

References

  1. ↑ Goto M, Yamauchi T, Kamiya N, Miyahara I, Yoshimura T, Mihara H, Kurihara T, Hirotsu K, Esaki N. Crystal structure of a homolog of mammalian serine racemase from Schizosaccharomyces pombe. J Biol Chem. 2009 Sep 18;284(38):25944-52. Epub 2009 Jul 28. PMID:19640845 doi:10.1074/jbc.M109.010470

1v71, resolution 1.70Å

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