Sandbox Reserved 1500

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<Structure load='5hfg' size='450' frame='true' align='right' caption='' scene='Insert optional scene name here' />
== Structural highlights ==
== Structural highlights ==
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<Structure load='5hfg' size='450' frame='true' align='right' caption='' scene='Insert optional scene name here' />
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== Nature ==
== Nature ==

Revision as of 15:46, 11 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

PDB ID 5hfg

Drag the structure with the mouse to rotate

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.
Secondary structure:
Figure 1: 5HFG secondary structure.
Figure 1: 5HFG secondary structure.[1]
,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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. [2]

Secondary structure

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

Tertiary structure

Monomeric assembly composition. 5hfg is one distinct polypeptide molecule. [3]



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. [4] 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.

Relevance

Click to see a sample scene created with SAT by Group, and to see a transparent representation of the protein.


References

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