2cth: Difference between revisions

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==CYTOCHROME C3 FROM DESULFOVIBRIO VULGARIS HILDENBOROUGH==
==CYTOCHROME C3 FROM DESULFOVIBRIO VULGARIS HILDENBOROUGH==
<StructureSection load='2cth' size='340' side='right' caption='[[2cth]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
<StructureSection load='2cth' size='340' side='right'caption='[[2cth]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2cth]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris_str._hildenborough Desulfovibrio vulgaris str. hildenborough]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cth 1cth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CTH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CTH FirstGlance]. <br>
<table><tr><td colspan='2'>[[2cth]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_vulgaris_str._Hildenborough Desulfovibrio vulgaris str. Hildenborough]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cth 1cth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CTH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 1.67&#8491;</td></tr>
<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=2cth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cth OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cth RCSB], [http://www.ebi.ac.uk/pdbsum/2cth PDBsum]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=2cth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cth OCA], [https://pdbe.org/2cth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cth RCSB], [https://www.ebi.ac.uk/pdbsum/2cth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cth ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CYC3_DESVH CYC3_DESVH]] Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin.  
[https://www.uniprot.org/uniprot/CYC3_DESVH CYC3_DESVH] Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ct/2cth_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ct/2cth_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata 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=2cth ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Cytochrome c|Cytochrome c]]
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Desulfovibrio vulgaris str. hildenborough]]
[[Category: Desulfovibrio vulgaris str. Hildenborough]]
[[Category: Carrondo, M A]]
[[Category: Large Structures]]
[[Category: Dauter, Z]]
[[Category: Carrondo MA]]
[[Category: Matias, P M]]
[[Category: Dauter Z]]
[[Category: Morais, J]]
[[Category: Matias PM]]
[[Category: Simoes, P]]
[[Category: Morais J]]
[[Category: Wilson, K]]
[[Category: Simoes P]]
[[Category: Electron transport]]
[[Category: Wilson K]]

Latest revision as of 09:42, 9 August 2023

CYTOCHROME C3 FROM DESULFOVIBRIO VULGARIS HILDENBOROUGHCYTOCHROME C3 FROM DESULFOVIBRIO VULGARIS HILDENBOROUGH

Structural highlights

2cth is a 2 chain structure with sequence from Desulfovibrio vulgaris str. Hildenborough. This structure supersedes the now removed PDB entry 1cth. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.67Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CYC3_DESVH Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2cth, resolution 1.67Å

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