1wo2 Summary


Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion

The structure was published by Qian, M., Ajandouz, E.H., Payan, F., and Nahoum, V., in 2005 in a paper entitled "Molecular Basis of the Effects of Chloride Ion on the Acid-Base Catalyst in the Mechanism of Pancreatic alpha-Amylase" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.01 Å and deposited in 2004.

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

The PDB entry contains the structure of Alpha-amylase, pancreatic. 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 Alpha-amylase, pancreatic 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) Alpha-amylase, pancreatic 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 cation bindingsearch chloride ion bindingsearch hydrolase activity, acting on glycosyl bondssearch hydrolase activitysearch calcium ion bindingsearch alpha-amylase activitysearch metal ion bindingsearch carbohydrate metabolic processsearch metabolic processsearch carbohydrate catabolic 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