1amy Summary



The structure was published by Kadziola, A., Abe, J., Svensson, B., and Haser, R., in 1994 in a paper entitled "Crystal and molecular structure of barley alpha-amylase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 1994.

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

The PDB entry contains the structure of 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE. This molecule has the UniProt identifier P04063 (AMY2_HORVU)search. The sample contained 403 residues which is 100% of the natural sequence. Out of 403 residues 403 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 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE P04063 (25-427) (AMY2_HORVU)search Hordeum vulgaresearch 100% 403 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P04063 (25 - 427) 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE Hordeum vulgare

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P04063) alpha-Amylases, C-terminal beta-sheet domainsearch, Amylase, catalytic domainsearch Glycosidasessearch, Golgi alpha-mannosidase IIsearch PF00128: Alpha amylase, catalytic domainsearch, PF07821: Alpha-amylase C-terminal beta-sheet domainsearch

Chain ID Biological process (GO) Molecular function (GO)
A (P04063) carbohydrate metabolic processsearch metabolic processsearch calcium ion bindingsearch catalytic activitysearch cation bindingsearch alpha-amylase activitysearch hydrolase activitysearch metal ion bindingsearch hydrolase activity, acting on glycosyl bondssearch

Chain InterPro annotation
A Alpha amylasesearch Glycosyl hydrolase, family 13, catalytic domainsearch Glycosyl hydrolase, family 13, subfamily, catalytic domainsearch Alpha-amylase, C-terminal beta-sheetsearch Alpha-amylase, plantsearch Glycosyl hydrolase, family 13, all-betasearch Glycoside hydrolase, catalytic domainsearch Glycoside hydrolase, family 13search Glycoside hydrolase superfamilysearch