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4ixt
From Proteopedia
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| - | + | [[Image:4ixt.jpg|left|200px]] | |
| - | + | {{STRUCTURE_4ixt| PDB=4ixt | SCENE= }} | |
| - | + | ===Structure of a 37-fold mutant of halohydrin dehalogenase (HheC) bound to ethyl (R)-4-cyano-3-hydroxybutyrate=== | |
| - | + | ||
| + | ==About this Structure== | ||
| + | [[4ixt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IXT OCA]. | ||
| + | [[Category: Agrobacterium tumefaciens]] | ||
| + | [[Category: Breuer, M.]] | ||
| + | [[Category: Dijkstra, B W.]] | ||
| + | [[Category: Floor, R J.]] | ||
| + | [[Category: Hauer, B.]] | ||
| + | [[Category: Janssen, D B.]] | ||
| + | [[Category: Jekel, P A]] | ||
| + | [[Category: Schallmey, M.]] | ||
| + | [[Category: Wijma, H J.]] | ||
| + | [[Category: Atorvastatin synthesis]] | ||
| + | [[Category: Backbone change]] | ||
| + | [[Category: Coupled mutation]] | ||
| + | [[Category: Cyanolysis]] | ||
| + | [[Category: Dehalogenase]] | ||
| + | [[Category: Directed evolution]] | ||
| + | [[Category: Enantioselectivity change]] | ||
| + | [[Category: Lyase]] | ||
| + | [[Category: Proline-induced]] | ||
| + | [[Category: Protein engineering]] | ||
| + | [[Category: Short-chain dehydrogenase/reductase enzyme superfamily]] | ||
| + | [[Category: Synergistic mutation]] | ||
| + | [[Category: Thermostability]] | ||
Revision as of 14:02, 20 February 2013
Structure of a 37-fold mutant of halohydrin dehalogenase (HheC) bound to ethyl (R)-4-cyano-3-hydroxybutyrate
About this Structure
4ixt is a 2 chain structure with sequence from Agrobacterium tumefaciens. Full crystallographic information is available from OCA.
Categories: Agrobacterium tumefaciens | Breuer, M. | Dijkstra, B W. | Floor, R J. | Hauer, B. | Janssen, D B. | Jekel, P A | Schallmey, M. | Wijma, H J. | Atorvastatin synthesis | Backbone change | Coupled mutation | Cyanolysis | Dehalogenase | Directed evolution | Enantioselectivity change | Lyase | Proline-induced | Protein engineering | Short-chain dehydrogenase/reductase enzyme superfamily | Synergistic mutation | Thermostability
