1bya Summary

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CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS

The structure was published by Mikami, B., Degano, M., Hehre, E.J., and Sacchettini, J.C., in 1994 in a paper entitled "Crystal structures of soybean beta-amylase reacted with beta-maltose and maltal: active site components and their apparent roles in catalysis." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1994.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of BETA-AMYLASE. This molecule has the UniProt identifier P10538 (AMYB_SOYBN)search. The sample contained 495 residues which is 100% of the natural sequence. Out of 495 residues 491 were observed and are deposited in the PDB.

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 is most likely monomeric.

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-AMYLASE P10538 (2-496) (AMYB_SOYBN)search Glycine maxsearch 99% 495 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P10538 (2 - 496) BETA-AMYLASE Glycine max

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P10538) Amylase, catalytic domainsearch Glycosidasessearch PF01373: Glycosyl hydrolase family 14search

Chain ID Biological process (GO) Molecular function (GO)
A (P10538) metabolic processsearch carbohydrate metabolic processsearch polysaccharide catabolic processsearch beta-amylase activitysearch hydrolase activity, acting on glycosyl bondssearch hydrolase activitysearch

Chain InterPro annotation
A Glycoside hydrolase, family 14B, plantsearch Glycoside hydrolase, family 14search Glycoside hydrolase, catalytic domainsearch Glycoside hydrolase superfamilysearch Glycoside hydrolase, family 14, conserved sitesearch