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2c3p

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<StructureSection load='2c3p' size='340' side='right'caption='[[2c3p]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
<StructureSection load='2c3p' size='340' side='right'caption='[[2c3p]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2c3p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_africanus Desulfovibrio africanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C3P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C3P FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2c3p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfocurvibacter_africanus Desulfocurvibacter africanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C3P 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=1TP:1-(2-{(2S,4R,5R)-3-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-2-[(1S)-1-CARBOXY-1-HYDROXYETHYL]-4-METHYL-1,3-THIAZOLIDIN-5-YL}ETHOXY)-1,1,3,3-TETRAHYDROXY-1LAMBDA~5~-DIPHOSPHOX-1-EN-2-IUM+3-OXIDE'>1TP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 2.33&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b0p|1b0p]], [[1kek|1kek]], [[2pda|2pda]], [[2c3m|2c3m]], [[2c3o|2c3o]], [[2c3u|2c3u]], [[2c3y|2c3y]], [[2c42|2c42]]</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=1TP:1-(2-{(2S,4R,5R)-3-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-2-[(1S)-1-CARBOXY-1-HYDROXYETHYL]-4-METHYL-1,3-THIAZOLIDIN-5-YL}ETHOXY)-1,1,3,3-TETRAHYDROXY-1LAMBDA~5~-DIPHOSPHOX-1-EN-2-IUM+3-OXIDE'>1TP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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/Pyruvate_synthase Pyruvate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.7.1 1.2.7.1] </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=2c3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c3p OCA], [https://pdbe.org/2c3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c3p RCSB], [https://www.ebi.ac.uk/pdbsum/2c3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c3p 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=2c3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c3p OCA], [http://pdbe.org/2c3p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c3p RCSB], [http://www.ebi.ac.uk/pdbsum/2c3p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c3p ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/P94692_DESAF P94692_DESAF]] Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (By similarity).[PIRNR:PIRNR000159]
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[https://www.uniprot.org/uniprot/PFOR_DESAF PFOR_DESAF] Catalyzes the ferredoxin-dependent oxidative decarboxylation of pyruvate. Required for the transfer of electrons from pyruvate to ferredoxin (PubMed:9294422, PubMed:7612653). Ferredoxin I and ferredoxin II, which are single 4Fe-4S cluster ferredoxins are the most effective electron carriers of POR (PubMed:7612653).<ref>PMID:7612653</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Desulfovibrio africanus]]
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[[Category: Desulfocurvibacter africanus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Pyruvate synthase]]
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[[Category: Cavazza C]]
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[[Category: Cavazza, C]]
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[[Category: Chabriere E]]
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[[Category: Chabriere, E]]
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[[Category: Contreras-Martel C]]
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[[Category: Contreras-Martel, C]]
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[[Category: Fontecilla-Camps JC]]
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[[Category: Fontecilla-Camps, J C]]
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[[Category: Hatchikian EC]]
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[[Category: Hatchikian, E C]]
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[[Category: Pieulle L]]
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[[Category: Pieulle, L]]
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[[Category: 4fe-4]]
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[[Category: Electron transport]]
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[[Category: Iron]]
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[[Category: Iron-sulfur]]
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[[Category: Iron-sulfur cluster]]
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[[Category: Metal-binding]]
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[[Category: Oxidoreductase]]
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[[Category: Pyruvate catabolism]]
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[[Category: Tpp-dependent enzyme]]
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Current revision

CRYSTAL STRUCTURE OF THE FREE RADICAL INTERMEDIATE OF PYRUVATE:FERREDOXIN OXIDOREDUCTASE FROM Desulfovibrio africanus

PDB ID 2c3p

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