3fsm
From Proteopedia
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===CRYSTAL STRUCTURE OF A CHEMICALLY SYNTHESIZED 203 AMINO ACID 'COVALENT DIMER' [L-Ala51,D-Ala51'] HIV-1 PROTEASE MOLECULE=== | ===CRYSTAL STRUCTURE OF A CHEMICALLY SYNTHESIZED 203 AMINO ACID 'COVALENT DIMER' [L-Ala51,D-Ala51'] HIV-1 PROTEASE MOLECULE=== | ||
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| + | The line below this paragraph, {{ABSTRACT_PUBMED_22158985}}, adds the Publication Abstract to the page | ||
| + | (as it appears on PubMed at http://www.pubmed.gov), where 22158985 is the PubMed ID number. | ||
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| + | {{ABSTRACT_PUBMED_22158985}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[3fsm]] is a 1 chain structure of [[Virus protease]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FSM OCA]. | |
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| + | ==See Also== | ||
| + | *[[Virus protease]] | ||
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| + | ==Reference== | ||
| + | <ref group="xtra">PMID:022158985</ref><references group="xtra"/> | ||
[[Category: HIV-1 retropepsin]] | [[Category: HIV-1 retropepsin]] | ||
[[Category: Kent, S B.H.]] | [[Category: Kent, S B.H.]] | ||
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[[Category: Beta-sheet]] | [[Category: Beta-sheet]] | ||
[[Category: Covalent dimer]] | [[Category: Covalent dimer]] | ||
| - | [[Category: Hydrolase]] | ||
[[Category: Hydrolase-hydrolase inhibitor complex]] | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 20 09:09:03 2010'' | ||
Revision as of 05:45, 11 January 2012
Contents |
CRYSTAL STRUCTURE OF A CHEMICALLY SYNTHESIZED 203 AMINO ACID 'COVALENT DIMER' [L-Ala51,D-Ala51'] HIV-1 PROTEASE MOLECULE
Template:ABSTRACT PUBMED 22158985
About this Structure
3fsm is a 1 chain structure of Virus protease. Full crystallographic information is available from OCA.
See Also
Reference
- Torbeev VY, Raghuraman H, Hamelberg D, Tonelli M, Westler WM, Perozo E, Kent SB. Protein conformational dynamics in the mechanism of HIV-1 protease catalysis. Proc Natl Acad Sci U S A. 2011 Dec 27;108(52):20982-7. Epub 2011 Dec 8. PMID:22158985 doi:10.1073/pnas.1111202108
