3l6b: Difference between revisions

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New page: '''Unreleased structure''' The entry 3l6b is ON HOLD Authors: Smith, M.A., Mack, V., Ebneth, A., Moraes, I, Felicetti, B., Wood, M., Schonfeld, D, Mather, O, Cesura, A, Barker, J.J. De...
 
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'''Unreleased structure'''


The entry 3l6b is ON HOLD
==X-ray crystal structure of human serine racemase in complex with malonate a potent inhibitor==
 
<StructureSection load='3l6b' size='340' side='right'caption='[[3l6b]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
Authors: Smith, M.A., Mack, V., Ebneth, A., Moraes, I, Felicetti, B., Wood, M., Schonfeld, D, Mather, O, Cesura, A, Barker, J.J.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[3l6b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L6B FirstGlance]. <br>
Description: X-RAY CRYSTAL STRUCTURE OF HUMAN SERINE RACEMASE IN COMPLEX WITH MALONATE A POTENT INHIBITOR
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 30 13:49:17 2009''
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3l6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l6b OCA], [https://pdbe.org/3l6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l6b RCSB], [https://www.ebi.ac.uk/pdbsum/3l6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l6b ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SRR_HUMAN SRR_HUMAN] Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.<ref>PMID:11054547</ref> <ref>PMID:20106978</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l6/3l6b_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3l6b ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Barker J]]
[[Category: Cesura A]]
[[Category: Ebneth A]]
[[Category: Felicetti B]]
[[Category: Mack V]]
[[Category: Moraes I]]
[[Category: Smith MA]]

Latest revision as of 09:40, 3 April 2024

X-ray crystal structure of human serine racemase in complex with malonate a potent inhibitorX-ray crystal structure of human serine racemase in complex with malonate a potent inhibitor

Structural highlights

3l6b is a 1 chain structure with sequence from Homo sapiens. 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

SRR_HUMAN Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.[1] [2]

Evolutionary Conservation

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

References

  1. ↑ De Miranda J, Santoro A, Engelender S, Wolosker H. Human serine racemase: moleular cloning, genomic organization and functional analysis. Gene. 2000 Oct 3;256(1-2):183-8. PMID:11054547
  2. ↑ Smith MA, Mack V, Ebneth A, Moraes I, Felicetti B, Wood M, Schonfeld D, Mather O, Cesura A, Barker J. The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding. J Biol Chem. 2010 Apr 23;285(17):12873-81. Epub 2010 Jan 27. PMID:20106978 doi:10.1074/jbc.M109.050062

3l6b, resolution 1.50Å

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