1sox
From Proteopedia
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|PDB= 1sox |SIZE=350|CAPTION= <scene name='initialview01'>1sox</scene>, resolution 1.9Å | |PDB= 1sox |SIZE=350|CAPTION= <scene name='initialview01'>1sox</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MO:MOLYBDENUM+ATOM'>MO</scene>, <scene name='pdbligand=MTE:PHOSPHONIC+ACIDMONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,7,8A,9,10,10A-HEXAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL)ESTER'>MTE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Sulfite_oxidase Sulfite oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.1 1.8.3.1] </span> | |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sox OCA], [http://www.ebi.ac.uk/pdbsum/1sox PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sox RCSB]</span> | ||
}} | }} | ||
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[[Category: Rees, D C.]] | [[Category: Rees, D C.]] | ||
[[Category: Schindelin, H.]] | [[Category: Schindelin, H.]] | ||
| - | [[Category: EPE]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: MO]] | ||
| - | [[Category: MTE]] | ||
| - | [[Category: SO4]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: sulfite oxidation]] | [[Category: sulfite oxidation]] | ||
| - | ''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 23:45:01 2008'' |
Revision as of 20:45, 30 March 2008
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , | ||||||
| Activity: | Sulfite oxidase, with EC number 1.8.3.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SULFITE OXIDASE FROM CHICKEN LIVER
Overview
The molybdenum-containing enzyme sulfite oxidase catalyzes the conversion of sulfite to sulfate, the terminal step in the oxidative degradation of cysteine and methionine. Deficiency of this enzyme in humans usually leads to major neurological abnormalities and early death. The crystal structure of chicken liver sulfite oxidase at 1.9 A resolution reveals that each monomer of the dimeric enzyme consists of three domains. At the active site, the Mo is penta-coordinated by three sulfur ligands, one oxo group, and one water/hydroxo. A sulfate molecule adjacent to the Mo identifies the substrate binding pocket. Four variants associated with sulfite oxidase deficiency have been identified: two mutations are near the sulfate binding site, while the other mutations occur within the domain mediating dimerization.
About this Structure
1SOX is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase., Kisker C, Schindelin H, Pacheco A, Wehbi WA, Garrett RM, Rajagopalan KV, Enemark JH, Rees DC, Cell. 1997 Dec 26;91(7):973-83. PMID:9428520
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