3l2m Summary


X-ray Crystallographic Analysis of Pig Pancreatic Alpha-Amylase with Alpha-cyclodextrin

The structure was published by Larson, S.B., Day, J.S., and McPherson, A., in 2010 in a paper entitled "X-ray crystallographic analyses of pig pancreatic alpha-amylase with limit dextrin, oligosaccharide, and alpha-cyclodextrin." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.97 Å and deposited in 2009.

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

The PDB entry contains the structure of Pancreatic 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 Pancreatic alpha-amylase P00690 (16-511) (AMYP_PIG)search Sus scrofasearch 100% 496 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00690 (16 - 511) Pancreatic alpha-amylase Sus scrofa

Chain Structural classification (CATH) Sequence family (Pfam)
A (P00690) 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 cation bindingsearch metal ion bindingsearch calcium ion bindingsearch hydrolase activity, acting on glycosyl bondssearch alpha-amylase activitysearch hydrolase activitysearch chloride ion bindingsearch 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