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Beta-Amylase from Bacillus cereus var. mycoides in Complex with alpha-EBG

The structure was published by Oyama, T., Miyake, H., Kusunoki, M., and Nitta, Y., in 2003 in a paper entitled "Crystal Structures of beta-Amylase from Bacillus cereus var. mycoides in Complexes with Substrate Analogs and Affinity-Labeling Reagents" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2002.

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 P36924 (31-546) (AMYB_BACCE)search Bacillus cereussearch 100% 516 100%
B Beta-amylase P36924 (31-546) (AMYB_BACCE)search Bacillus cereussearch 100% 516 100%
C Beta-amylase P36924 (31-546) (AMYB_BACCE)search Bacillus cereussearch 100% 516 100%
D Beta-amylase P36924 (31-546) (AMYB_BACCE)search Bacillus cereussearch 100% 516 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P36924 (31 - 546) Beta-amylase Bacillus cereus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (P36924) Starch-binding domainsearch, Amylase, catalytic domainsearch Glycosidasessearch, Immunoglobulinssearch PF00686: Starch binding domainsearch, PF01373: Glycosyl hydrolase family 14search

Chain ID Molecular function (GO) Biological process (GO)
A, B, C, D (P36924) beta-amylase activitysearch starch bindingsearch hydrolase activitysearch metal ion bindingsearch hydrolase activity, acting on glycosyl bondssearch polysaccharide catabolic processsearch carbohydrate metabolic processsearch metabolic processsearch polysaccharide metabolic processsearch

Chain InterPro annotation
A, B, C, D Glycoside hydrolase, family 14A, bacterialsearch Glycoside hydrolase, family 14search Carbohydrate binding module family 20search Glycoside hydrolase, catalytic domainsearch Immunoglobulin-like foldsearch Glycoside hydrolase superfamilysearch Glycoside hydrolase, family 14, conserved sitesearch