2oc5

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==Crystal structure of a ferritin-like protein (pmt1231) from prochlorococcus marinus str. mit 9313 at 1.68 A resolution==
==Crystal structure of a ferritin-like protein (pmt1231) from prochlorococcus marinus str. mit 9313 at 1.68 A resolution==
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<StructureSection load='2oc5' size='340' side='right' caption='[[2oc5]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
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<StructureSection load='2oc5' size='340' side='right'caption='[[2oc5]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2oc5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Promm Promm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OC5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OC5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2oc5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Promm Promm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OC5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr>
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</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=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NP_895059.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=74547 PROMM])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NP_895059.1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=74547 PROMM])</td></tr>
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<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=2oc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oc5 OCA], [http://pdbe.org/2oc5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2oc5 RCSB], [http://www.ebi.ac.uk/pdbsum/2oc5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2oc5 ProSAT], [http://www.topsan.org/Proteins/JCSG/2oc5 TOPSAN]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2oc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oc5 OCA], [https://pdbe.org/2oc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oc5 RCSB], [https://www.ebi.ac.uk/pdbsum/2oc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oc5 ProSAT], [https://www.topsan.org/Proteins/JCSG/2oc5 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ALDEC_PROMM ALDEC_PROMM]] Catalyzes the decarbonylation of fatty aldehydes to alkanes. Requires the presence of ferredoxin, ferredoxin reductase and NADPH for in vitro decarbonylase activity (By similarity). Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane.<ref>PMID:20671186</ref>
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[[https://www.uniprot.org/uniprot/ALDEC_PROMM ALDEC_PROMM]] Catalyzes the decarbonylation of fatty aldehydes to alkanes. Requires the presence of ferredoxin, ferredoxin reductase and NADPH for in vitro decarbonylase activity (By similarity). Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane.<ref>PMID:20671186</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oc/2oc5_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oc/2oc5_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Promm]]
[[Category: Promm]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]

Revision as of 12:52, 9 June 2021

Crystal structure of a ferritin-like protein (pmt1231) from prochlorococcus marinus str. mit 9313 at 1.68 A resolution

PDB ID 2oc5

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