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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.81 Classification:OXYGEN TRANSPORT Release Date:2018-02-28 Deposition Date:2017-02-14 Revision Date: Molecular Weight:18808.0 Macromolecule Type:Protein Residue Count:154 Atom Site Count:1325 DOI:10.2210/pdb5uta/pdb
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  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.2 Classification:TOXIN Release Date:2018-02-28 Deposition Date:2017-09-01 Revision Date: Molecular Weight:8319.94 Macromolecule Type:Protein Residue Count:76 Atom Site Count:556 DOI:10.2210/pdb6ava/pdb
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.47 Classification:OXIDOREDUCTASE Release Date:2018-02-28 Deposition Date:2016-12-23 Revision Date: Molecular Weight:59370.73 Macromolecule Type:Protein Residue Count:574 Atom Site Count:3321 DOI:10.2210/pdb5wva/pdb Abstract: Bioconversion is useful to produce optically pure enantiomers in the pharmaceutical industry, thereby avoiding problems with side reactions during organic synthesis processes. A short-chain dehydrogenase/reductase from Serratia marcescens BCRC 10948 (SmSDR) can stereoselectively convert 1-(3-hydroxyphenyl)-2-(methylamino) ethanone (HPMAE) into (R)-phenylephrine [(R)-PE], which is marketed medically as a nasal decongestant agent. The whole-cell conversion process for the synthesis of (R)-PE using SmSDR was reported to have an unexpectedly low conversion rate. We reported the crystal structure of the SmSDR and designed profitable variants to improve the enzymatic activity by structure-guided approach. Several important residues in the structure were observed to form hydrophobic clusters that stabilize the mobile loops surrounding the pocket. Of these, Phe98 and Phe202 face toward each other and connect the upper curvature from the two arms (i.e., the α7 helix and loopβ4-α4). The mutant structure of the double substitutions (F98YF202Y) exhibited a hydrogen bond between the curvatures that stabilizes the flexible arms. Site-directed mutagenesis characterization revealed that the mutations (F98Y, F98YF202Y, and F98YF202L) of the flexible loops that stabilize the region exhibited a higher transformation activity toward HPMAE. Together, our results suggest a robust structure-guided approach that can be used to generate a valuable engineered variant for pharmaceutical applications.
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.55 Classification:HYDROLASE Release Date:2018-02-28 Deposition Date:2017-01-18 Revision Date: Molecular Weight:27835.41 Macromolecule Type:Protein Residue Count:245 Atom Site Count:1663 DOI:10.2210/pdb5mwa/pdb
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.22 Classification:RNA Release Date:2018-02-28 Deposition Date:2017-02-25 Revision Date: Molecular Weight:23147.22 Macromolecule Type:RNA Residue Count:71 Atom Site Count:1518 DOI:10.2210/pdb5uza/pdb
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.64 Classification:TRANSFERASE Release Date:2018-02-28 Deposition Date:2017-02-08 Revision Date: Molecular Weight:43428.41 Macromolecule Type:Protein Residue Count:372 Atom Site Count:2874 DOI:10.2210/pdb5n3b/pdb
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.14 Classification:STRUCTURAL PROTEIN Release Date:2018-02-28 Deposition Date:2017-03-22 Revision Date: Molecular Weight:36464.48 Macromolecule Type:Protein Residue Count:325 Atom Site Count:2375 DOI:10.2210/pdb5xcb/pdb
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.78 Classification:OXYGEN TRANSPORT Release Date:2018-02-28 Deposition Date:2017-02-14 Revision Date: Molecular Weight:18383.9 Macromolecule Type:Protein Residue Count:154 Atom Site Count:1277 DOI:10.2210/pdb5utb/pdb
Data Types:
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.54 Classification:OXIDOREDUCTASE Release Date:2018-02-28 Deposition Date:2017-02-20 Revision Date: Molecular Weight:43712.79 Macromolecule Type:Protein Residue Count:393 Atom Site Count:3086 DOI:10.2210/pdb5uvb/pdb
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  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.77 Classification:TRANSFERASE Release Date:2018-02-28 Deposition Date:2017-02-08 Revision Date: Molecular Weight:43432.43 Macromolecule Type:Protein Residue Count:372 Atom Site Count:2991 DOI:10.2210/pdb5n3c/pdb
Data Types:
  • Tabular Data
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