1q0e: Difference between revisions
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|PDB= 1q0e |SIZE=350|CAPTION= <scene name='initialview01'>1q0e</scene>, resolution 1.15Å | |PDB= 1q0e |SIZE=350|CAPTION= <scene name='initialview01'>1q0e</scene>, resolution 1.15Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q0e OCA], [http://www.ebi.ac.uk/pdbsum/1q0e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q0e RCSB]</span> | |||
}} | }} | ||
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[[Category: Hasnain, S S.]] | [[Category: Hasnain, S S.]] | ||
[[Category: Hough, M A.]] | [[Category: Hough, M A.]] | ||
[[Category: atomic resolution]] | [[Category: atomic resolution]] | ||
[[Category: bovine]] | [[Category: bovine]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:07:04 2008'' | ||
Revision as of 23:07, 30 March 2008
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| , resolution 1.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Atomic resolution (1.15 ) crystal structure of bovine copper, zinc superoxide dismutase
OverviewOverview
Copper zinc superoxide dismutase (CuZnSOD) forms a crucial component of the cellular response to oxidative stress by catalyzing the dismutation of the superoxide radical to hydrogen peroxide and water. Mutations in human CuZnSOD are associated with the development of familial amyotrophic lateral sclerosis (motor neuron disease). We have determined the structure of fully reduced bovine CuZnSOD to 1.15 A, the only atomic resolution structure for an intact CuZnSOD and one of only a small number for metalloproteins. For the first time, both subunits have been captured with the three coordinate Cu(I) ligation required by the generally accepted catalytic mechanism, where dismutation of the superoxide radical occurs via reduction of Cu. Furthermore, the improved resolution compared to previous studies (to 1.65 A) has allowed a more detailed examination of the metal center environment and its associated water network in the active site channel, facilitating the analysis of potential proton transfer routes.
About this StructureAbout this Structure
1Q0E is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 A., Hough MA, Hasnain SS, Structure. 2003 Aug;11(8):937-46. PMID:12906825
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