1e5l
From Proteopedia
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[[Image:1e5l.png|left|200px]] | [[Image:1e5l.png|left|200px]] | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1e5l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Magnaporthe_grisea Magnaporthe grisea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E5L OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:11080625</ref><references group="xtra"/> | + | <ref group="xtra">PMID:11080625</ref><ref group="xtra">PMID:10771443</ref><references group="xtra"/> |
[[Category: Magnaporthe grisea]] | [[Category: Magnaporthe grisea]] | ||
[[Category: Johansson, E.]] | [[Category: Johansson, E.]] | ||
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[[Category: Schneider, G.]] | [[Category: Schneider, G.]] | ||
[[Category: Steffens, J J.]] | [[Category: Steffens, J J.]] | ||
| - | [[Category: Alpha-aminoadipate pathway]] | + | [[Category: Alpha- aminoadipate pathway]] |
[[Category: Lysine biosynthesis]] | [[Category: Lysine biosynthesis]] | ||
| + | [[Category: Oxidoreductase]] | ||
[[Category: Saccharopine reductase]] | [[Category: Saccharopine reductase]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 21:01:59 2009'' | ||
Revision as of 20:43, 14 March 2011
APO SACCHAROPINE REDUCTASE FROM MAGNAPORTHE GRISEA
Template:ABSTRACT PUBMED 11080625
About this Structure
1e5l is a 2 chain structure with sequence from Magnaporthe grisea. Full crystallographic information is available from OCA.
Reference
- Johansson E, Steffens JJ, Lindqvist Y, Schneider G. Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis. Structure. 2000 Oct 15;8(10):1037-47. PMID:11080625
- Johansson E, Steffens JJ, Emptage M, Lindqvist Y, Schneider G. Cloning, expression, purification and crystallization of saccharopine reductase from Magnaporthe grisea. Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):662-4. PMID:10771443 doi:10.1107/s0907444900003735
