1p1v
From Proteopedia
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{{STRUCTURE_1p1v| PDB=1p1v | SCENE= }} | {{STRUCTURE_1p1v| PDB=1p1v | SCENE= }} | ||
===Crystal Structure of FALS-associated human Copper-Zinc Superoxide Dismutase (CuZnSOD) Mutant D125H to 1.4A=== | ===Crystal Structure of FALS-associated human Copper-Zinc Superoxide Dismutase (CuZnSOD) Mutant D125H to 1.4A=== | ||
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{{ABSTRACT_PUBMED_12649272}} | {{ABSTRACT_PUBMED_12649272}} | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: Amyotrophic lateral sclerosis, due to SOD1 deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147450 147450]] | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[1p1v]] is a 3 chain structure of [[Superoxide Dismutase]] with sequence 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=1P1V OCA]. | |
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| + | ==See Also== | ||
| + | *[[Superoxide Dismutase|Superoxide Dismutase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:012649272</ref><references group="xtra"/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Superoxide dismutase]] | [[Category: Superoxide dismutase]] | ||
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[[Category: Bound anion at copper site]] | [[Category: Bound anion at copper site]] | ||
[[Category: Cuznsod peroxidation mechanism]] | [[Category: Cuznsod peroxidation mechanism]] | ||
| - | + | [[Category: Oxidoreductase]] | |
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Revision as of 16:15, 27 July 2012
Contents |
Crystal Structure of FALS-associated human Copper-Zinc Superoxide Dismutase (CuZnSOD) Mutant D125H to 1.4A
Template:ABSTRACT PUBMED 12649272
About this Structure
1p1v is a 3 chain structure of Superoxide Dismutase with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Elam JS, Malek K, Rodriguez JA, Doucette PA, Taylor AB, Hayward LJ, Cabelli DE, Valentine JS, Hart PJ. An alternative mechanism of bicarbonate-mediated peroxidation by copper-zinc superoxide dismutase: rates enhanced via proposed enzyme-associated peroxycarbonate intermediate. J Biol Chem. 2003 Jun 6;278(23):21032-9. Epub 2003 Mar 20. PMID:12649272 doi:10.1074/jbc.M300484200
