1hlq

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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=1hlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hlq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hlq RCSB], [http://www.ebi.ac.uk/pdbsum/1hlq PDBsum]</span></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=1hlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hlq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hlq RCSB], [http://www.ebi.ac.uk/pdbsum/1hlq PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/HIP_RHOFE HIP_RHOFE]] Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria. Competent in photosynthetic electron transfer to oxidized cytochrome bc1 complex via the membrane-bound c-type tetraheme.<ref>PMID:7574702</ref> [:]<ref>PMID:8001683</ref> <ref>PMID:7498498</ref> <ref>PMID:8692932</ref> <ref>PMID:10076014</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 16:15, 25 December 2014

CRYSTAL STRUCTURE OF RHODOFERAX FERMENTANS HIGH POTENTIAL IRON-SULFUR PROTEIN REFINED TO 1.45 A

1hlq, resolution 1.45Å

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