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2kgj
From Proteopedia
(Difference between revisions)
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| + | [[Image:2kgj.jpg|left|200px]] | ||
| - | The | + | <!-- |
| + | The line below this paragraph, containing "STRUCTURE_2kgj", creates the "Structure Box" on the page. | ||
| + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
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| + | {{STRUCTURE_2kgj| PDB=2kgj | SCENE= }} | ||
| - | + | ===Solution structure of parvulin domain of PpiD from E.Coli=== | |
| - | Description: Solution structure of parvulin domain of PpiD from E.Coli | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | + | <!-- |
| + | The line below this paragraph, {{ABSTRACT_PUBMED_19866485}}, adds the Publication Abstract to the page | ||
| + | (as it appears on PubMed at http://www.pubmed.gov), where 19866485 is the PubMed ID number. | ||
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| + | {{ABSTRACT_PUBMED_19866485}} | ||
| + | |||
| + | ==About this Structure== | ||
| + | 2KGJ is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KGJ OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | <ref group="xtra">PMID:19866485</ref><references group="xtra"/> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Peptidylprolyl isomerase]] | ||
| + | [[Category: Jakob, R P.]] | ||
| + | [[Category: Weininger, U.]] | ||
| + | [[Category: Cell inner membrane]] | ||
| + | [[Category: Cell membrane]] | ||
| + | [[Category: Isomerase]] | ||
| + | [[Category: Membrane]] | ||
| + | [[Category: Parvulin]] | ||
| + | [[Category: Prolyl isomerase]] | ||
| + | [[Category: Rotamase]] | ||
| + | [[Category: Stress response]] | ||
| + | [[Category: Transmembrane]] | ||
| + | |||
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 20 15:06:25 2010'' | ||
Revision as of 13:06, 20 January 2010
Solution structure of parvulin domain of PpiD from E.Coli
Template:ABSTRACT PUBMED 19866485
About this Structure
2KGJ is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA.
Reference
- Weininger U, Jakob RP, Kovermann M, Balbach J, Schmid FX. The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity. Protein Sci. 2010 Jan;19(1):6-18. PMID:19866485 doi:10.1002/pro.277
Page seeded by OCA on Wed Jan 20 15:06:25 2010
