4iie Summary

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Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with calystegine B(2)

The structure was published by Suzuki, K., Sumitani, J., Nam, Y.W., et al., Wakagi, T., Kawaguchi, T., and Fushinobu, S., in 2013 in a paper entitled "Crystal structures of glycoside hydrolase family 3 beta-glucosidase 1 from Aspergillus aculeatus" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2012.

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

This PDB entry contains multiple copies of the structure of Beta-glucosidase 1.

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 1 P48825 (20-860) (BGL1_ASPAC)search Aspergillus aculeatussearch 100% 841 99%
B Beta-glucosidase 1 P48825 (20-860) (BGL1_ASPAC)search Aspergillus aculeatussearch 100% 841 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P48825 (20 - 860) Beta-glucosidase 1 Aspergillus aculeatus

Chain Sequence family (Pfam)
A, B (P48825) PF00933: Glycosyl hydrolase family 3 N terminal domainsearch, PF01915: Glycosyl hydrolase family 3 C-terminal domainsearch, PF14310: Fibronectin type III-like domainsearch

Chain ID Biological process (GO) Molecular function (GO)
A, B (P48825) polysaccharide catabolic processsearch carbohydrate metabolic processsearch cellulose catabolic processsearch metabolic processsearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch hydrolase activitysearch hydrolase activity, acting on glycosyl bondssearch beta-glucosidase activitysearch

Chain InterPro annotation
A, B Glycoside hydrolase, family 3, N-terminalsearch Glycoside hydrolase family 3 C-terminal domainsearch Glycoside hydrolase superfamilysearch Glycoside hydrolase, family 3, active sitesearch Fibronectin type III-like domainsearch Glycoside hydrolase family 3search