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3aa3
From Proteopedia
(Difference between revisions)
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| + | [[Image:3aa3.jpg|left|200px]] | ||
| - | The | + | <!-- |
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| + | {{STRUCTURE_3aa3| PDB=3aa3 | SCENE= }} | ||
| - | + | ===A52L E. coli RNase HI=== | |
| - | Description: A52L E. coli RNase HI | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | + | <!-- |
| + | The line below this paragraph, {{ABSTRACT_PUBMED_20423323}}, adds the Publication Abstract to the page | ||
| + | (as it appears on PubMed at http://www.pubmed.gov), where 20423323 is the PubMed ID number. | ||
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| + | {{ABSTRACT_PUBMED_20423323}} | ||
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| + | ==About this Structure== | ||
| + | 3AA3 is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AA3 OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | <ref group="xtra">PMID:20423323</ref><references group="xtra"/> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Ribonuclease H]] | ||
| + | [[Category: Takano, K.]] | ||
| + | [[Category: Cavity]] | ||
| + | [[Category: Endonuclease]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Magnesium]] | ||
| + | [[Category: Metal-binding]] | ||
| + | [[Category: Nuclease]] | ||
| + | [[Category: Stability]] | ||
| + | |||
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 6 06:03:38 2010'' | ||
Revision as of 02:54, 6 October 2010
A52L E. coli RNase HI
Template:ABSTRACT PUBMED 20423323
About this Structure
3AA3 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Tanaka M, Chon H, Angkawidjaja C, Koga Y, Takano K, Kanaya S. Protein core adaptability: crystal structures of the cavity-filling variants of Escherichia coli RNase HI. Protein Pept Lett. 2010 Sep;17(9):1163-9. PMID:20423323
Page seeded by OCA on Wed Oct 6 06:03:38 2010
Categories: Escherichia coli | Ribonuclease H | Takano, K. | Cavity | Endonuclease | Hydrolase | Magnesium | Metal-binding | Nuclease | Stability
