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4pg1

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==Insights into Substrate and Metal Binding from the Crystal Structure of Cyanobacterial Aldehyde Deformylating Oxygenase with Substrate Bound==
==Insights into Substrate and Metal Binding from the Crystal Structure of Cyanobacterial Aldehyde Deformylating Oxygenase with Substrate Bound==
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<StructureSection load='4pg1' size='340' side='right' caption='[[4pg1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='4pg1' size='340' side='right'caption='[[4pg1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4pg1]] 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=4PG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PG1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4pg1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Prochlorococcus_marinus_str._MIT_9313 Prochlorococcus marinus str. MIT 9313]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PG1 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=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=Y39:(1S,2S)-2-NONYLCYCLOPROPANECARBOXYLIC+ACID'>Y39</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=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=Y39:(1S,2S)-2-NONYLCYCLOPROPANECARBOXYLIC+ACID'>Y39</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pg0|4pg0]], [[4pgi|4pgi]]</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=4pg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pg1 OCA], [https://pdbe.org/4pg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pg1 RCSB], [https://www.ebi.ac.uk/pdbsum/4pg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pg1 ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PMT_1231 ([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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Octadecanal_decarbonylase Octadecanal decarbonylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.5 4.1.99.5] </span></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=4pg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pg1 OCA], [http://pdbe.org/4pg1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pg1 RCSB], [http://www.ebi.ac.uk/pdbsum/4pg1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pg1 ProSAT]</span></td></tr>
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</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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Octadecanal decarbonylase]]
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[[Category: Large Structures]]
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[[Category: Promm]]
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[[Category: Prochlorococcus marinus str. MIT 9313]]
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[[Category: Buer, B C]]
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[[Category: Buer BC]]
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[[Category: Das, D]]
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[[Category: Das D]]
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[[Category: Marsh, E N.G]]
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[[Category: Marsh ENG]]
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[[Category: Paul, B]]
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[[Category: Paul B]]
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[[Category: Stuckey, J A]]
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[[Category: Stuckey JA]]
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[[Category: Alpha-helix]]
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[[Category: Hydrocarbon production]]
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[[Category: Non-heme di-iron protein]]
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[[Category: Oxidoreductase]]
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Revision as of 13:00, 1 February 2023

Insights into Substrate and Metal Binding from the Crystal Structure of Cyanobacterial Aldehyde Deformylating Oxygenase with Substrate Bound

PDB ID 4pg1

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