1ua3 Summary


Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides

The structure was published by Payan, F. and Qian, M., in 2003 in a paper entitled "Crystal Structure of the Pig Pancreatic alpha-Amylase Complexed with Malto-Oligosaccharides" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.01 Å and deposited in 2003.

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

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