4IXT

Structure of a 37-fold mutant of halohydrin dehalogenase (HheC) bound to ethyl (R)-4-cyano-3-hydroxybutyrate

Summary for 4IXT

• Entry DOI: 10.2210/pdb4ixt/pdb
• Related: 4IXW 4IY1
• Descriptor: Halohydrin dehalogenase, ethyl (3R)-4-cyano-3-hydroxybutanoate, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: thermostability, synergistic mutations, coupled mutations, proline-induced, backbone changes, enantioselectivity changes, directed evolution, protein engineering, short-chain dehydrogenase/reductase enzyme superfamily, cyanolysis, dehalogenase, atorvastatin synthesis, lyase
• Biological source: Rhizobium radiobacter (Agrobacterium tumefaciens)
• Total number of polymer chains: 2
• Total formula weight: 55875.43

Authors

Floor, R.J.,Schallmey, M.,Hauer, B.,Breuer, M.,Jekel, P.A.,Wijma, H.J.,Dijkstra, B.W.,Janssen, D.B. (deposition date: 2013-01-28, release date: 2013-02-20, Last modification date: 2023-09-20)

• Primary citation: Schallmey, M.,Floor, R.J.,Hauer, B.,Breuer, M.,Jekel, P.A.,Wijma, H.J.,Dijkstra, B.W.,Janssen, D.B.; Biocatalytic and structural properties of a highly engineered halohydrin dehalogenase.; Chembiochem, 14:870-881, 2013; PubMed: 23585096; DOI: 10.1002/cbic.201300005

Experimental method

X-RAY DIFFRACTION (2.49 Å)