This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2hg4
From Proteopedia
(Difference between revisions)
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | [[2hg4]] is a 6 chain structure | + | [[2hg4]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HG4 OCA]. |
==See Also== | ==See Also== | ||
| Line 14: | Line 14: | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:016844787</ref><ref group="xtra">PMID:015518537 | + | <ref group="xtra">PMID:016844787</ref><ref group="xtra">PMID:015518537</ref><references group="xtra"/> |
[[Category: 6-deoxyerythronolide-B synthase]] | [[Category: 6-deoxyerythronolide-B synthase]] | ||
[[Category: Saccharopolyspora erythraea]] | [[Category: Saccharopolyspora erythraea]] | ||
Revision as of 08:52, 20 October 2012
Contents |
Structure of the ketosynthase-acyltransferase didomain of module 5 from DEBS.
Template:ABSTRACT PUBMED 16844787
About this Structure
2hg4 is a 6 chain structure with sequence from Saccharopolyspora erythraea. Full crystallographic information is available from OCA.
See Also
Reference
- Tang Y, Kim CY, Mathews II, Cane DE, Khosla C. The 2.7-Angstrom crystal structure of a 194-kDa homodimeric fragment of the 6-deoxyerythronolide B synthase. Proc Natl Acad Sci U S A. 2006 Jul 25;103(30):11124-9. Epub 2006 Jul 14. PMID:16844787
- Kim CY, Alekseyev VY, Chen AY, Tang Y, Cane DE, Khosla C. Reconstituting modular activity from separated domains of 6-deoxyerythronolide B synthase. Biochemistry. 2004 Nov 9;43(44):13892-8. PMID:15518537 doi:10.1021/bi048418n
