1uko Summary


Crystal structure of soybean beta-amylase mutant substituted at surface region

The structure was published by Kang, Y.N., Adachi, M., Mikami, B., and Utsumi, S., in 2003 in a paper entitled "Change in the crystal packing of soybean beta-amylase mutants substituted at a few surface amino acid residues" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2003.

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

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

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 98%
B Beta-amylase P10538 (2-496) (AMYB_SOYBN)search Glycine maxsearch 99% 495 98%
C Beta-amylase P10538 (2-496) (AMYB_SOYBN)search Glycine maxsearch 99% 495 98%
D Beta-amylase P10538 (2-496) (AMYB_SOYBN)search Glycine maxsearch 99% 495 98%

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, B, C, D (P10538) Amylase, catalytic domainsearch Glycosidasessearch PF01373: Glycosyl hydrolase family 14search

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

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