3voc Summary


Crystal structure of the catalytic domain of beta-amylase from paenibacillus polymyxa

A publication describing this structure is not available. The depositing authors are Nishimura, S.search; Fujioka, T.search; Nakaniwa, T.search; Tada, T.search

This crystal structure was determined using X-ray diffraction at a resolution of 1.95 Å and deposited in 2012.

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

The PDB entry contains the structure of Beta/alpha-amylase. This molecule has the UniProt identifier P21543 (AMYB_PAEPO)search. The sample contained 419 residues which is < 90% of the natural sequence. Out of 419 residues 416 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/alpha-amylase P21543 (36-454) (AMYB_PAEPO)search Paenibacillus polymyxasearch < 90% 419 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P21543 (36 - 454) Beta/alpha-amylase Paenibacillus polymyxa

Chain Sequence family (Pfam)
A Glycosyl hydrolase family 14search

Chain ID Biological process (GO) Molecular function (GO)
A (P21543) polysaccharide metabolic processsearch polysaccharide catabolic processsearch carbohydrate metabolic processsearch beta-amylase activitysearch

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