Sandbox Reserved 1500

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	Global Symmetry: Asymmetric - C1		Global Symmetry: Asymmetric - C1
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	Global Stoichiometry: Monomer - A		Global Stoichiometry: Monomer - A
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	Its theoretical weight is 25.29 KDa		Its theoretical weight is 25.29 KDa

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Revision as of 17:15, 10 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.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. Click the 3D button (when editing, above the wikitext box) to insert Jmol. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

Contents 1 Structural highlights 1.1 Primary structure 1.2 Secondary structure 1.3 Tertiary structure 2 Nature 3 Function 4 Disease 5 Relevance 6 References

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance

Global Symmetry: Asymmetric - C1

Global Stoichiometry: Monomer - A

Its theoretical weight is 25.29 KDa

Primary structure

5hfg is a 1 chain structure of 238 amino acids. ^[1]

Secondary structure

The structure of 5hfg mainly consists in alpha helix (12) , beta sheets (4), you can check the 3D view here.

Tertiary structure

Monomeric assembly composition. 5hfg is one distinct polypeptide molecule. ^[2]

spinqualitylabelsall models PDB ID 5hfg Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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. ^[3] It has no bound ligands and no modified residues. Sequence domains:

   Thioredoxin-like superfamily
   DSBA-like thioredoxin domain 

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

1. ↑ https://www.rcsb.org/structure/5HFG
2. ↑ https://www.ebi.ac.uk/pdbe/entry/pdb/5HFG
3. ↑ https://www.rcsb.org/structure/5HFG