1E55

Crystal structure of the inactive mutant Monocot (Maize ZMGlu1) beta-glucosidase ZMGluE191D in complex with the competitive inhibitor dhurrin

Summary for 1E55

Related1E1E 1E1F 1E4L 1E4N 1E56
DescriptorBETA-GLUCOSIDASE, BETA-D-GLUCOSE, (2S)-HYDROXY(4-HYDROXYPHENYL)ETHANENITRILE, ... (4 entities in total)
Functional Keywordsglycoside hydrolase, beta-glucosidase, family 1, retention of the anomeric configuration, inactive mutant e191d, complex with dhurrin, hydrolase
Biological sourceZEA MAYS (MAIZE)
Total number of polymer chains2
Total molecular weight117575.45
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: 2019-01-16)
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
PubMed: 11106394 (PDB entries with the same primary citation)
DOI: 10.1073/pnas.97.25.13555
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers11 0.5% 3.4% 2.4%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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