1wdr Summary


The role of an inner loop in the catalytic mechanism of soybean beta-amylase

The structure was published by Kang, Y.N., Tanabe, A., Adachi, M., Utsumi, S., and Mikami, B., in 2005 in a paper entitled "Structural analysis of threonine 342 mutants of soybean beta-amylase: role of a conformational change of the inner loop in the catalytic mechanism." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.35 Å and deposited in 2004.

The experimental data on which the structure is based was also 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 493 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) polysaccharide catabolic processsearch carbohydrate metabolic processsearch metabolic processsearch beta-amylase activitysearch hydrolase activitysearch hydrolase activity, acting on glycosyl bondssearch

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