8rxn

<StructureSection load='8rxn' size='340' side='right' caption='[[8rxn]], [[Resolution|resolution]] 1.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[8rxn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29579 Atcc 29579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RXN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=8RXN FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=8rxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rxn OCA], [http://pdbe.org/8rxn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=8rxn RCSB], [http://www.ebi.ac.uk/pdbsum/8rxn PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/RUBR_DESVH RUBR_DESVH]] Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. Electron acceptor for cytoplasmic lactate dehydrogenase.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rx/8rxn_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

X-ray data have been recorded from crystals of rubredoxin derived from the bacterium Desulfovibrio vulgaris to a resolution of 1.0 A using in part synchrotron radiation and in part X-rays from a sealed-tube Mo K alpha source. In both cases an imaging-plate scanner was used as detector. The space group of the crystals is P2(1) with cell dimensions a = 19.97, b = 41.45, c = 24.41 A and beta = 108.3 degrees. The overall merging R(I) factor between symmetry-related reflections was 5.8%. The model was refined by least-squares minimization initially with stereochemical restraints to an R factor of 16.4%. Only atomic positional parameters and isotropic temperature factors for non-H atoms were used in the refinement. There were 18,532 independent X-ray observations for a total of 1916 atomic parameters. A round of unrestrained refinement gave an R factor of 16.0%, acceptable geometry for more than 90% of the protein atoms, but emphasized the disorder inherent in eight of the residues. A final round of restrained refinement gave an R factor of 14.7%. Three of the 389 protein atoms in the molecule, in the side chain of Lys2, have been assigned zero occupancy in the model. A total of eight atoms in three side chains have been assigned two conformations, giving 393 protein atomic sites in the model. In addition there is one Fe atom, a sulfate ion and 102 water sites. 339 H atoms were included at their calculated positions, which were not refined. There is clear evidence for anisotropic thermal motion. This has not been incorporated in the present model.

Refinement of rubredoxin from Desulfovibrio vulgaris at 1.0 A with and without restraints.,Dauter Z, Sieker LC, Wilson KS Acta Crystallogr B. 1992 Feb 1;48 ( Pt 1):42-59. PMID:1616692<ref>PMID:1616692</ref>

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== References ==

[[Category: Atcc 29579]]

[[Category: Dauter, Z]]

[[Category: Sieker, L]]

[[Category: Wilson, K]]