1hxj Summary



The structure was published by Zouhar, J., Vevodova, J., Marek, J., Damborsky, J., Su, X.-D., and Brzobohaty, B., in 2001 in a paper entitled "Insights into the functional architecture of the catalytic center of a maize beta-glucosidase Zm-p60.1" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.05 Å and deposited in 2001.

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

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

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 (60-566) (HGGL1_MAIZE)search Zea mayssearch 90% 507 97%
B BETA-GLUCOSIDASE P49235 (60-566) (HGGL1_MAIZE)search Zea mayssearch 90% 507 97%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P49235 (60 - 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 Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (P49235) hydrolase activity, hydrolyzing O-glycosyl compoundssearch hydrolase activitysearch beta-glucosidase activitysearch hydrolase activity, acting on glycosyl bondssearch carbohydrate metabolic processsearch metabolic processsearch cytokinin-activated signaling pathwaysearch chloroplastsearch plastidsearch

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