4l2c: Difference between revisions

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{{STRUCTURE_4l2c|  PDB=4l2c  |  SCENE=  }}
===X-ray structure of the C57R mutant of the iron superoxide dismutase from Pseudoalteromonas haloplanktis (crystal form I)===
{{ABSTRACT_PUBMED_24440460}}


==Function==
==X-ray structure of the C57R mutant of the iron superoxide dismutase from Pseudoalteromonas haloplanktis (crystal form I)==
[[http://www.uniprot.org/uniprot/SODF_PSEHT SODF_PSEHT]] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.<ref>PMID:16713057</ref>
<StructureSection load='4l2c' size='340' side='right'caption='[[4l2c]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4l2c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudoalteromonas_haloplanktis Pseudoalteromonas haloplanktis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L2C FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.66&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900006:trehalose'>PRD_900006</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=4l2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l2c OCA], [https://pdbe.org/4l2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l2c RCSB], [https://www.ebi.ac.uk/pdbsum/4l2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l2c ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SODF_PSET1 SODF_PSET1] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.<ref>PMID:16713057</ref>  


==About this Structure==
==See Also==
[[4l2c]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L2C OCA].
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:024440460</ref><references group="xtra"/><references/>
__TOC__
[[Category: Superoxide dismutase]]
</StructureSection>
[[Category: Krauss, I Russo.]]
[[Category: Large Structures]]
[[Category: Merlino, A.]]
[[Category: Pseudoalteromonas haloplanktis]]
[[Category: Sica, F.]]
[[Category: Merlino A]]
[[Category: C57r mutant]]
[[Category: Russo Krauss I]]
[[Category: Oxidoreductase]]
[[Category: Sica F]]
[[Category: Superoxide dismutase]]

Latest revision as of 15:16, 1 March 2024

X-ray structure of the C57R mutant of the iron superoxide dismutase from Pseudoalteromonas haloplanktis (crystal form I)X-ray structure of the C57R mutant of the iron superoxide dismutase from Pseudoalteromonas haloplanktis (crystal form I)

Structural highlights

4l2c is a 4 chain structure with sequence from Pseudoalteromonas haloplanktis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.66Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SODF_PSET1 Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.[1]

See Also

References

  1. Castellano I, Di Maro A, Ruocco MR, Chambery A, Parente A, Di Martino MT, Parlato G, Masullo M, De Vendittis E. Psychrophilic superoxide dismutase from Pseudoalteromonas haloplanktis: biochemical characterization and identification of a highly reactive cysteine residue. Biochimie. 2006 Oct;88(10):1377-89. Epub 2006 Apr 27. PMID:16713057 doi:http://dx.doi.org/S0300-9084(06)00055-1

4l2c, resolution 1.66Å

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