3bsh Summary

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Barley alpha-amylase isozyme 1 (AMY1) double mutant Y105A/Y380A in complex with inhibitor acarbose

The structure was published by Nielsen, M.M., Seo, E.S., Bozonnet, S., et al., Robert, X., Haser, R., and Svensson, B., in 2008 in a paper entitled "Multi-site substrate binding and interplay in barley alpha-amylase 1" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.0 Å and deposited in 2007.

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

The PDB entry contains the structure of Alpha-amylase type A isozyme. This molecule has the UniProt identifier P00693 (AMY1_HORVU)search. The sample contained 414 residues which is 100% of the natural sequence. Out of 414 residues 404 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 type A isozyme P00693 (25-438) (AMY1_HORVU)search Hordeum vulgaresearch 98% 414 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00693 (25 - 438) Alpha-amylase type A isozyme Hordeum vulgare

Chain Structural classification (CATH) Sequence family (Pfam)
A (P00693) Glycosidasessearch, Golgi alpha-mannosidase IIsearch PF00128: Alpha amylase, catalytic domainsearch, PF07821: Alpha-amylase C-terminal beta-sheet domainsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P00693) calcium ion bindingsearch cation bindingsearch catalytic activitysearch alpha-amylase activitysearch hydrolase activity, acting on glycosyl bondssearch metal ion bindingsearch hydrolase activitysearch carbohydrate metabolic processsearch metabolic processsearch extracellular regionsearch extracellular spacesearch

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