1v08 Summary



The structure was published by Verdoucq, L., Moriniere, J., Bevan, D.R., et al., Vasella, A., Henrissat, B., and Czjzek, M., in 2004 in a paper entitled "Structural Determinants of Substrate Specificity in Family 1 Beta-Glucosidases: Novel Insights from the Crystal Structure of Sorghum Dhurrinase-1, a Plant Beta-Glucosidase with Strict Specificity, in Complex with its Natural Substrate" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2004.

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 95%
B BETA-GLUCOSIDASE P49235 (55-566) (HGGL1_MAIZE)search Zea mayssearch 90% 512 95%

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

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