6taa Summary



The structure was published by Swift, H.J., Brady, L., Derewenda, Z.S., et al., Dodson, G.G., Turkenburg, J.P., and Wilkinson, A.J., in 1991 in a paper entitled "Structure and molecular model refinement of Aspergillus oryzae (TAKA) alpha-amylase: an application of the simulated-annealing method." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1992.

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

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

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