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<StructureSection load='1cry' size='340' side='right'caption='[[1cry]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='1cry' size='340' side='right'caption='[[1cry]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1cry]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_19567 Atcc 19567]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CRY FirstGlance]. <br>
<table><tr><td colspan='2'>[[1cry]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CRY FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cry OCA], [https://pdbe.org/1cry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cry RCSB], [https://www.ebi.ac.uk/pdbsum/1cry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cry ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cry OCA], [https://pdbe.org/1cry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cry RCSB], [https://www.ebi.ac.uk/pdbsum/1cry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cry ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CYC2_BLAVI CYC2_BLAVI]] Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria.  
[https://www.uniprot.org/uniprot/CYC2_BLAVI CYC2_BLAVI] Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cry ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cry ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
An automatic molecular-replacement procedure has been applied to solve the crystal structure of cytochrome c(2) from Rhodopseudomonas viridis. The structure was solved on the basis of the structure of tuna cytochrome c as a search model using an automatic processing program system, AUTOMR. The refinements by molecular dynamics and restrained least-squares methods result in a current crystallographic R factor of 0.219 for diffraction data at 3 A resolution.
Application of an automatic molecular-replacement procedure to crystal structure analysis of cytochrome c2 from Rhodopseudomonas viridis.,Miki K, Sogabe S, Uno A, Ezoe T, Kasai N, Saeda M, Matsuura Y, Miki M Acta Crystallogr D Biol Crystallogr. 1994 May 1;50(Pt 3):271-5. PMID:15299438<ref>PMID:15299438</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1cry" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 19567]]
[[Category: Blastochloris viridis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Miki, K]]
[[Category: Miki K]]
[[Category: Sogabe, S]]
[[Category: Sogabe S]]

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