Sandbox Reserved 1500
From Proteopedia
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'''5hfg''' is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HFG OCA]. For a guided tour on the structure components use [https://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HFG FirstGlance] | '''5hfg''' is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HFG OCA]. For a guided tour on the structure components use [https://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HFG FirstGlance] | ||
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== Nature == | == Nature == | ||
| - | '''5hfg''' is a Dsb-family protein, | + | '''5hfg''' is a Dsb-family protein, from Pseudomonas Aeruginosa. This family of proteins is mainly used to oxidize and reduce cysteine residues of substrate proteins. Most enzymes from Dsb-family catalyze disulfide formation in periplasmic or secreted substrate proteins. |
== Function == | == Function == | ||
Revision as of 22:11, 8 January 2019
| This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543. |
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Contents |
Structural highlights
5hfg is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance
Headline text
|
Nature
5hfg is a Dsb-family protein, from Pseudomonas Aeruginosa. This family of proteins is mainly used to oxidize and reduce cysteine residues of substrate proteins. Most enzymes from Dsb-family catalyze disulfide formation in periplasmic or secreted substrate proteins.
Function
This protein has a disulfide oxidoreductase activity.
Disease
Relevance
This is a sample scene created with SAT to by Group, and another to make of the protein.
</StructureSection>
References
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
