1sda
From Proteopedia
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|PDB= 1sda |SIZE=350|CAPTION= <scene name='initialview01'>1sda</scene>, resolution 2.5Å | |PDB= 1sda |SIZE=350|CAPTION= <scene name='initialview01'>1sda</scene>, resolution 2.5Å | ||
|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=NO2:NITRITE+ION'>NO2</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=1sda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sda OCA], [http://www.ebi.ac.uk/pdbsum/1sda PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sda RCSB]</span> | ||
}} | }} | ||
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[[Category: Smith, C D.]] | [[Category: Smith, C D.]] | ||
[[Category: Woerd, M Van Der.]] | [[Category: Woerd, M Van Der.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: NO2]] | ||
| - | [[Category: ZN]] | ||
[[Category: oxidoreductase(copper)]] | [[Category: oxidoreductase(copper)]] | ||
| - | ''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 23:40:33 2008'' |
Revision as of 20:40, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF PEROXYNITRITE-MODIFIED BOVINE CU,ZN SUPEROXIDE DISMUTASE
Overview
The crystal structure of bovine Cu,Zn superoxide dismutase modified with peroxynitrite (ONOO-) was determined by X-ray diffraction, utilizing the existing three-dimensional model of the native structure deposited in the Brookhaven Protein Data Bank (J. A. Tainer et al., J. Mol. Biol. 160, 181-217, 1982). The native structure and the modified derivative were refined to R factors of 19.0 and 18.7% respectively using diffraction data from 6.0 to 2.5 A. The major result after reaction with peroxynitrite was the appearance of electron density 1.45 A from a single epsilon carbon of Tyr-108, the only tyrosine residue in the sequence. Tyr-108 is a solvent-exposed residue 18 A from the copper atom in the active site. The electron density was consistent with nitration of Tyr-108 at one of the epsilon carbons to form 3-nitrotyrosine. We propose that the nitration occurs in solution by transfer of a nitronium-like species from the active site on one superoxide dismutase dimer to the Tyr-108 of a second dimer.
About this Structure
1SDA is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Crystal structure of peroxynitrite-modified bovine Cu,Zn superoxide dismutase., Smith CD, Carson M, van der Woerd M, Chen J, Ischiropoulos H, Beckman JS, Arch Biochem Biophys. 1992 Dec;299(2):350-5. PMID:1444476
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