4IY1
Structure of a 37-fold mutant of halohydrin dehalogenase (HheC) with chloride bound
Summary for 4IY1
Entry DOI | 10.2210/pdb4iy1/pdb |
Related | 4IXT 4IXW |
Descriptor | Halohydrin dehalogenase, CHLORIDE ION (3 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 | 55789.17 |
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 Cited by PubMed: 23585096DOI: 10.1002/cbic.201300005 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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