1azv
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1azv |SIZE=350|CAPTION= <scene name='initialview01'>1azv</scene>, resolution 1.9Å | |PDB= 1azv |SIZE=350|CAPTION= <scene name='initialview01'>1azv</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> | + | |LIGAND= <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= SOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= SOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1azv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1azv OCA], [http://www.ebi.ac.uk/pdbsum/1azv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1azv RCSB]</span> | ||
}} | }} | ||
| Line 33: | Line 36: | ||
[[Category: Pellegrini, M.]] | [[Category: Pellegrini, M.]] | ||
[[Category: Valentine, J S.]] | [[Category: Valentine, J S.]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: ZN]] | ||
[[Category: familial amyotrophic lateral sclerosis mutant]] | [[Category: familial amyotrophic lateral sclerosis mutant]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: superoxide acceptor]] | [[Category: superoxide acceptor]] | ||
| - | ''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 18:50:47 2008'' |
Revision as of 15:50, 30 March 2008
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | SOD1 (Homo sapiens) | ||||||
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)
Contents |
Overview
The X-ray crystal structure of a human copper/zinc superoxide dismutase mutant (G37R CuZnSOD) found in some patients with the inherited form of Lou Gehrig's disease (FALS) has been determined to 1.9 angstroms resolution. The two SOD subunits have distinct environments in the crystal and are different in structure at their copper binding sites. One subunit (subunit[intact]) shows a four-coordinate ligand geometry of the copper ion, whereas the other subunit (subunit[broken]) shows a three-coordinate geometry of the copper ion. Also, subunit(intact) displays higher atomic displacement parameters for backbone atoms ((B) = 30 +/- 10 angstroms2) than subunit(broken) ((B) = 24 +/- 11 angstroms2). This structure is the first CuZnSOD to show large differences between the two subunits. Factors that may contribute to these differences are discussed and a possible link of a looser structure to FALS is suggested.
Disease
Known disease associated with this structure: Amyotrophic lateral sclerosis, due to SOD1 deficiency OMIM:[147450]
About this Structure
1AZV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis., Hart PJ, Liu H, Pellegrini M, Nersissian AM, Gralla EB, Valentine JS, Eisenberg D, Protein Sci. 1998 Mar;7(3):545-55. PMID:9541385
Page seeded by OCA on Sun Mar 30 18:50:47 2008
