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Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>
= <Biological unit>

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( jV3 / Jmol ) *1
PDB ID1e55  sequence information (FASTA format)   
RELATED PDB ID1e1e, 1e1f, 1e4l, 1e4n, 1e56
DescriptorBETA-GLUCOSIDASE (E.C.3.2.1.21)
TitleCRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE ZMGLU1) BETA-GLUCOSIDASE ZMGLUE191D IN COMPLEX WITH THE COMPETITIVE INHIBITOR DHURRIN
Functional KeywordsGLYCOSIDE HYDROLASE, BETA-GLUCOSIDASE, FAMILY 1, RETENTION OF THE ANOMERIC CONFIGURATION, INACTIVE MUTANT E191D, COMPLEX WITH DHURRIN
Biological source (MAIZE)
Cellular location [UNP - P49235] Plastid, chloroplast
Organ source [UNP - P49235] Shoot
[UNP - P49235] Coleoptile
Total number of polymer chains2
Total molecular weight117576.8 (the details in Structural Details Page)
AuthorsCzjzek, M. , Cicek, M. , Bevan, D.R. , Zamboni, V. , Henrissat, B. , Esen, A. (deposition date : 2000-07-18, release date : 2000-12-11)
Primary citationCzjzek, 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 - , 2000.(PubMed : 11106394)  (DOI: 10.1073/PNAS.97.25.13555)
Experimental methodX-RAY DIFFRACTION ( 2.0[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P49235 ) , eF-site , KEGG ( EC 3.2.1.21 ) , PISA