1e55 Summary

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CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE ZMGLU1) BETA-GLUCOSIDASE ZMGLUE191D IN COMPLEX WITH THE COMPETITIVE INHIBITOR DHURRIN

The structure was published by Czjzek, M., Cicek, M., Zamboni, V., Bevan, D.R., Henrissat, B., and Esen, A., in 2000 in a paper entitled "The Mechanism of Substrate (Aglycone) Specificity in Beta -Glucosidases is Revealed by Crystal Structures of Mutant Maize Beta -Glucosidase-Dimboa, -Dimboaglc, and -Dhurrin Complexes" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2000.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of BETA-GLUCOSIDASE.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A BETA-GLUCOSIDASE P49235 (55-566) (HGGL1_MAIZE)search Zea mayssearch 90% 512 96%
B BETA-GLUCOSIDASE P49235 (55-566) (HGGL1_MAIZE)search Zea mayssearch 90% 512 96%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P49235 (55 - 566) BETA-GLUCOSIDASE Zea mays

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P49235) Family 1 of glycosyl hydrolasesearch Glycosidasessearch PF00232: Glycosyl hydrolase family 1search

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A, B (P49235) carbohydrate metabolic processsearch metabolic processsearch cytokinin-activated signaling pathwaysearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch beta-glucosidase activitysearch hydrolase activity, acting on glycosyl bondssearch hydrolase activitysearch chloroplastsearch plastidsearch

Chain InterPro annotation
A, B Glycoside hydrolase, family 1search Glycoside hydrolase, catalytic domainsearch Glycoside hydrolase, superfamilysearch Glycoside hydrolase, family 1, active sitesearch