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3gqf
From Proteopedia
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===Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q=== | ===Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q=== | ||
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| - | <!-- | ||
| - | The line below this paragraph, {{ABSTRACT_PUBMED_19227972}}, adds the Publication Abstract to the page | ||
| - | (as it appears on PubMed at http://www.pubmed.gov), where 19227972 is the PubMed ID number. | ||
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| - | {{ABSTRACT_PUBMED_19227972}} | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
3GQF is a 6 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GQF OCA]. | 3GQF is a 6 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GQF OCA]. | ||
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| - | ==Reference== | ||
| - | <ref group="xtra">PMID:19227972</ref><references group="xtra"/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Superoxide dismutase]] | [[Category: Superoxide dismutase]] | ||
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[[Category: Zinc]] | [[Category: Zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 17 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 17 20:16:12 2009'' |
Revision as of 17:11, 17 June 2009
Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q
Disease
Known disease associated with this structure: Amyotrophic lateral sclerosis, due to SOD1 deficiency OMIM:[147450]
About this Structure
3GQF is a 6 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Page seeded by OCA on Wed Jun 17 20:16:12 2009
Categories: Homo sapiens | Superoxide dismutase | Hart, P J. | Schuermann, J P. | Winkler, D D. | Acetylation | Amyotrophic lateral sclerosis | Antioxidant | Copper | Cytoplasm | Disease mutation | Disulfide bond | Familial amyotrophic lateral sclerosis mutant | Human cu-zn superoxide dismutase | Metal-binding | Oxidoreductase | Phosphoprotein | Superoxide acceptor | Ubl conjugation | Zinc
