4pg0

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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='4pg0' size='340' side='right' caption='[[4pg0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='4pg0' size='340' side='right'caption='[[4pg0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4pg0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PG0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PG0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4pg0]] 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=4PG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PG0 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pg1|4pg1]], [[4pgi|4pgi]], [[4pgk|4pgk]]</td></tr>
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<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='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'>[https://proteopedia.org/fgij/fg.htm?mol=4pg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pg0 OCA], [https://pdbe.org/4pg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pg0 RCSB], [https://www.ebi.ac.uk/pdbsum/4pg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pg0 ProSAT]</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=4pg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pg0 OCA], [http://pdbe.org/4pg0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pg0 RCSB], [http://www.ebi.ac.uk/pdbsum/4pg0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pg0 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>
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<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: Buer, B C]]
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[[Category: Prochlorococcus marinus str. MIT 9313]]
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[[Category: Das, D]]
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[[Category: Buer BC]]
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[[Category: Marsh, E N.G]]
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[[Category: Das D]]
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[[Category: Paul, B]]
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[[Category: Marsh ENG]]
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[[Category: Stuckey, J A]]
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[[Category: Paul B]]
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[[Category: Alpha-helix]]
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[[Category: Stuckey JA]]
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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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Current revision

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

PDB ID 4pg0

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