1ose Summary

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Porcine pancreatic alpha-amylase complexed with acarbose

The structure was published by Gilles, C., Astier, J.P., Marchis-Mouren, G., Cambillau, C., and Payan, F., in 1996 in a paper entitled "Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 1996.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of PORCINE ALPHA-AMYLASE. This molecule has the UniProt identifier P00690 (AMYP_PIG)search. The sample contained 496 residues which is 100% of the natural sequence. Out of 496 residues 496 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 PORCINE ALPHA-AMYLASE P00690 (17-511) (AMYP_PIG)search Sus scrofasearch 100% 496 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00690 (17 - 511) PORCINE ALPHA-AMYLASE Sus scrofa

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P00690) alpha-Amylases, C-terminal beta-sheet domainsearch, Amylase, catalytic domainsearch Glycosidasessearch, Golgi alpha-mannosidase IIsearch PF00128: Alpha amylase, catalytic domainsearch, PF02806: Alpha amylase, C-terminal all-beta domainsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P00690) catalytic activitysearch metal ion bindingsearch hydrolase activitysearch cation bindingsearch hydrolase activity, acting on glycosyl bondssearch calcium ion bindingsearch chloride ion bindingsearch alpha-amylase activitysearch carbohydrate metabolic processsearch carbohydrate catabolic processsearch metabolic processsearch extracellular regionsearch extracellular spacesearch

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