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3lb8

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==Crystal structure of the covalent putidaredoxin reductase-putidaredoxin complex==
==Crystal structure of the covalent putidaredoxin reductase-putidaredoxin complex==
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<StructureSection load='3lb8' size='340' side='right' caption='[[3lb8]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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<StructureSection load='3lb8' size='340' side='right'caption='[[3lb8]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3lb8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LB8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LB8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3lb8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LB8 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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q1r|1q1r]], [[1oqq|1oqq]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1q1r|1q1r]], [[1oqq|1oqq]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">camA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886]), camA, camB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">camA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886]), camA, camB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</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=3lb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lb8 OCA], [http://pdbe.org/3lb8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lb8 RCSB], [http://www.ebi.ac.uk/pdbsum/3lb8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lb8 ProSAT]</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=3lb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lb8 OCA], [https://pdbe.org/3lb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lb8 RCSB], [https://www.ebi.ac.uk/pdbsum/3lb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lb8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CAMA_PSEPU CAMA_PSEPU]] The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.<ref>PMID:12011076</ref> [[http://www.uniprot.org/uniprot/PUTX_PSEPU PUTX_PSEPU]] The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.
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[[https://www.uniprot.org/uniprot/CAMA_PSEPU CAMA_PSEPU]] The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.<ref>PMID:12011076</ref> [[https://www.uniprot.org/uniprot/PUTX_PSEPU PUTX_PSEPU]] The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
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*[[Ferredoxin|Ferredoxin]]
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*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Bacillus fluorescens putidus flugge 1886]]
[[Category: Bacillus fluorescens putidus flugge 1886]]
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[[Category: Large Structures]]
[[Category: Sevrioukova, I F]]
[[Category: Sevrioukova, I F]]
[[Category: Covalently linked protein-protein complex]]
[[Category: Covalently linked protein-protein complex]]

Revision as of 12:32, 13 October 2021

Crystal structure of the covalent putidaredoxin reductase-putidaredoxin complex

PDB ID 3lb8

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