7taa Summary



The structure was published by Brzozowski, A.M. and Davies, G.J., in 1997 in a paper entitled "Structure of the Aspergillus oryzae alpha-amylase complexed with the inhibitor acarbose at 2.0 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.98 Å and deposited in 1997.

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

The PDB entry contains the structure of TAKA AMYLASE. This molecule has the UniProt identifier P0C1B3 (AMYA1_ASPOR)search. The sample contained 478 residues which is 100% of the natural sequence. Out of 478 residues 476 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 TAKA AMYLASE P0C1B3 (22-499) (AMYA1_ASPOR)search Aspergillus oryzae RIB40search 100% 478 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0C1B3 (22 - 499) TAKA AMYLASE Aspergillus oryzae

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P0C1B3) alpha-Amylases, C-terminal beta-sheet domainsearch, Amylase, catalytic domainsearch Glycosidasessearch, Golgi alpha-mannosidase IIsearch PF00128: Alpha amylase, catalytic domainsearch, PF09260: Domain of unknown function (DUF1966)search

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P0C1B3) cation bindingsearch calcium ion bindingsearch alpha-amylase activitysearch catalytic activitysearch metal ion bindingsearch hydrolase activitysearch hydrolase activity, acting on glycosyl bondssearch carbohydrate metabolic processsearch carbohydrate catabolic processsearch metabolic processsearch extracellular regionsearch cellular_componentsearch hyphal septin bandsearch cell wall-bounded periplasmic spacesearch spitzenkorpersearch fungal-type cell wallsearch cell septumsearch

Chain InterPro annotation
A Alpha amylasesearch Glycosyl hydrolase, family 13, catalytic domainsearch Glycosyl hydrolase, family 13, subfamily, catalytic domainsearch Alpha-amylase, fungisearch Glycosyl hydrolase, family 13, all-betasearch Glycoside hydrolase, catalytic domainsearch Alpha-amylase, domain of unknown function DUF1966, C-terminalsearch Glycoside hydrolase, family 13search Glycoside hydrolase superfamilysearch