1sos: Difference between revisions
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[[Image:1sos.gif|left|200px]] | [[Image:1sos.gif|left|200px]] | ||
'''ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE MUTANT RECOMBINANT HUMAN CU, ZN SUPEROXIDE DISMUTASE''' | {{Structure | ||
|PDB= 1sos |SIZE=350|CAPTION= <scene name='initialview01'>1sos</scene>, resolution 2.5Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</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] | |||
|GENE= | |||
}} | |||
'''ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE MUTANT RECOMBINANT HUMAN CU, ZN SUPEROXIDE DISMUTASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1SOS is a [ | 1SOS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1SOS with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb94_1.html Superoxide Dismutase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SOS OCA]. | ||
==Reference== | ==Reference== | ||
Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase., Parge HE, Hallewell RA, Tainer JA, Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):6109-13. PMID:[http:// | Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase., Parge HE, Hallewell RA, Tainer JA, Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):6109-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1463506 1463506] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase (superoxide acceptor)]] | [[Category: oxidoreductase (superoxide acceptor)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:07:44 2008'' | ||
Revision as of 15:07, 20 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE MUTANT RECOMBINANT HUMAN CU, ZN SUPEROXIDE DISMUTASE
OverviewOverview
Superoxide dismutase enzymes protect aerobic organisms from oxygen-mediated free-radical damage. Crystallographic structures of recombinant human Cu,Zn superoxide dismutase have been determined, refined, and analyzed at 2.5 A resolution for wild-type and a designed thermostable double-mutant enzyme (Cys-6----Ala, Cys-111----Ser). The 10 subunits (five dimers) in the crystallographic asymmetric unit form an unusual stable open lattice with 80-A-diameter channels. The 10 independently fit and refined subunits provide high accuracy, error analysis, and insights on loop conformations. There is a helix dipole interaction with the Zn site, and 14 residues form two or more structurally conserved side-chain to main-chain hydrogen bonds that appear critical to active-site architecture, loop conformation, and the increased stability resulting from the Cys-111----Ser mutation.
DiseaseDisease
Known disease associated with this structure: Amyotrophic lateral sclerosis, due to SOD1 deficiency OMIM:[147450]
About this StructureAbout this Structure
1SOS is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1SOS with [Superoxide Dismutase]. Full crystallographic information is available from OCA.
ReferenceReference
Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase., Parge HE, Hallewell RA, Tainer JA, Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):6109-13. PMID:1463506
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