1ppi Summary

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THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE. THE STRUCTURE OF THE COMPLEX OF A PANCREATIC ALPHA-AMYLASE WITH A CARBOHYDRATE INHIBITOR REFINED TO 2.2 ANGSTROMS RESOLUTION

The structure was published by Qian, M., Haser, R., Buisson, G., Duee, E., and Payan, F., in 1994 in a paper entitled "The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1994.

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

The PDB entry contains the structure of 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 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) 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 Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P00690) carbohydrate metabolic processsearch carbohydrate catabolic processsearch metabolic processsearch cation bindingsearch hydrolase activitysearch alpha-amylase activitysearch calcium ion bindingsearch catalytic activitysearch hydrolase activity, acting on glycosyl bondssearch metal ion bindingsearch chloride ion bindingsearch 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