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[[Image:1vkh.gif|left|200px]]


{{Structure
==CRYSTAL STRUCTURE OF A PUTATIVE SERINE HYDROLASE (YDR428C) FROM SACCHAROMYCES CEREVISIAE AT 1.85 A RESOLUTION==
|PDB= 1vkh |SIZE=350|CAPTION= <scene name='initialview01'>1vkh</scene>, resolution 1.85&Aring;
<StructureSection load='1vkh' size='340' side='right'caption='[[1vkh]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
<table><tr><td colspan='2'>[[1vkh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VKH FirstGlance]. <br>
|ACTIVITY=
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
|GENE= ydr428c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
<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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG0657 Aes]</span>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vkh OCA], [https://pdbe.org/1vkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vkh RCSB], [https://www.ebi.ac.uk/pdbsum/1vkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vkh ProSAT], [https://www.topsan.org/Proteins/JCSG/1vkh TOPSAN]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vkh OCA], [http://www.ebi.ac.uk/pdbsum/1vkh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vkh RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/KFA_YEAST KFA_YEAST] Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.[HAMAP-Rule:MF_03014]<ref>PMID:18205391</ref>
 
== Evolutionary Conservation ==
'''Crystal structure of putative serine hydrolase (ydr428c) from Saccharomyces cerevisiae at 1.85 A resolution'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vk/1vkh_consurf.spt"</scriptWhenChecked>
1VKH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VKH OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
Crystal structure of an alpha/beta serine hydrolase (YDR428C) from Saccharomyces cerevisiae at 1.85 A resolution., Arndt JW, Schwarzenbacher R, Page R, Abdubek P, Ambing E, Biorac T, Canaves JM, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Hornsby M, Klock HE, Koesema E, Kreusch A, Kuhn P, Jaroszewski L, Lesley SA, Levin I, McMullan D, McPhillips TM, Miller MD, Morse A, Moy K, Nigoghossian E, Ouyang J, Peti WS, Quijano K, Reyes R, Sims E, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, von Delft F, Wang X, West B, White A, Wolf G, Xu Q, Zagnitko O, Hodgson KO, Wooley J, Wilson IA, Proteins. 2005 Feb 15;58(3):755-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15624212 15624212]
</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=1vkh ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: JCSG, Joint Center for Structural Genomics.]]
[[Category: jcsg]]
[[Category: joint center for structural genomic]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: putative serine hydrolase]]
[[Category: structural genomic]]
[[Category: ydr428c]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:25:40 2008''

Latest revision as of 10:29, 9 October 2024

CRYSTAL STRUCTURE OF A PUTATIVE SERINE HYDROLASE (YDR428C) FROM SACCHAROMYCES CEREVISIAE AT 1.85 A RESOLUTIONCRYSTAL STRUCTURE OF A PUTATIVE SERINE HYDROLASE (YDR428C) FROM SACCHAROMYCES CEREVISIAE AT 1.85 A RESOLUTION

Structural highlights

1vkh is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

KFA_YEAST Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.[HAMAP-Rule:MF_03014][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. ↑ Wogulis M, Chew ER, Donohoue PD, Wilson DK. Identification of Formyl Kynurenine Formamidase and Kynurenine Aminotransferase from Saccharomyces cerevisiae Using Crystallographic, Bioinformatic and Biochemical Evidence. Biochemistry. 2008 Feb 12;47(6):1608-21. Epub 2008 Jan 19. PMID:18205391 doi:10.1021/bi701172v

1vkh, resolution 1.85Å

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