1y9a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='1y9a' size='340' side='right'caption='[[1y9a]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
<StructureSection load='1y9a' size='340' side='right'caption='[[1y9a]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1y9a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Enthi Enthi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Y9A FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1y9a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y9A FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.81&#8491;</td></tr>
-
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OHS:O-(CARBOXYSULFANYL)-4-OXO-L-HOMOSERINE'>OHS</scene></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OHS:O-(CARBOXYSULFANYL)-4-OXO-L-HOMOSERINE'>OHS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 ENTHI])</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=1y9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y9a OCA], [https://pdbe.org/1y9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y9a RCSB], [https://www.ebi.ac.uk/pdbsum/1y9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y9a ProSAT]</span></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] </span></td></tr>
+
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1y9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y9a OCA], [http://pdbe.org/1y9a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y9a RCSB], [http://www.ebi.ac.uk/pdbsum/1y9a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y9a ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/ADH1_ENTHI ADH1_ENTHI]] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.<ref>PMID:20102159</ref>
+
[https://www.uniprot.org/uniprot/ADH1_ENTHI ADH1_ENTHI] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.<ref>PMID:20102159</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 35: Line 33:
*[[Alcohol dehydrogenase|Alcohol dehydrogenase]]
*[[Alcohol dehydrogenase|Alcohol dehydrogenase]]
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
-
*[[Alcohol dehydrogenase from Entamoeba histolytica|Alcohol dehydrogenase from Entamoeba histolytica]]
 
-
*[[Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH|Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH]]
 
-
*[[Chimeras of alcohol dehydrogenases|Chimeras of alcohol dehydrogenases]]
 
-
*[[D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica|D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica]]
 
-
*[[Tetrameric alcohol dehydrogenases|Tetrameric alcohol dehydrogenases]]
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Enthi]]
+
[[Category: Entamoeba histolytica]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Burstein, Y]]
+
[[Category: Burstein Y]]
-
[[Category: Frolow, F]]
+
[[Category: Frolow F]]
-
[[Category: Goihberg, E]]
+
[[Category: Goihberg E]]
-
[[Category: Peretz, M]]
+
[[Category: Peretz M]]
-
[[Category: Shimon, L J]]
+
[[Category: Shimon LJ]]
-
[[Category: Metal-binding]]
+
-
[[Category: Nadp]]
+
-
[[Category: Oxidoreductase]]
+

Revision as of 08:01, 15 May 2024

Alcohol Dehydrogenase from Entamoeba histolotica in complex with cacodylate

PDB ID 1y9a

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools