1E55
Crystal structure of the inactive mutant Monocot (Maize ZMGlu1) beta-glucosidase ZMGluE191D in complex with the competitive inhibitor dhurrin
Summary for 1E55
Entry DOI | 10.2210/pdb1e55/pdb |
Related | 1E1E 1E1F 1E4L 1E4N 1E56 |
Descriptor | BETA-GLUCOSIDASE, beta-D-glucopyranose, (2S)-HYDROXY(4-HYDROXYPHENYL)ETHANENITRILE, ... (4 entities in total) |
Functional Keywords | glycoside hydrolase, beta-glucosidase, family 1, retention of the anomeric configuration, inactive mutant e191d, complex with dhurrin, hydrolase |
Biological source | ZEA MAYS (MAIZE) |
Total number of polymer chains | 2 |
Total formula weight | 117575.45 |
Authors | Czjzek, M.,Cicek, M.,Bevan, D.R.,Zamboni, V.,Henrissat, B.,Esen, A. (deposition date: 2000-07-18, release date: 2000-12-11, Last modification date: 2023-12-13) |
Primary citation | Czjzek, M.,Cicek, M.,Zamboni, V.,Bevan, D.R.,Henrissat, B.,Esen, A. The mechanism of substrate (aglycone) specificity in beta-glucosidases is revealed by crystal structures of mutant maize beta-glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes. Proc. Natl. Acad. Sci. U.S.A., 97:13555-13560, 2000 Cited by PubMed: 11106394DOI: 10.1073/pnas.97.25.13555 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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