1mxg Summary


Crystal Strucutre of a (Ca,Zn)-dependent alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei in complex with acarbose

The structure was published by Linden, A., Mayans, O., Meyer-Klaucke, W., Antranikian, G., and Wilmanns, M., in 2003 in a paper entitled "Differential Regulation of a Hyperthermophilic alpha-Amylase with a Novel (Ca,Zn) Two-metal Center by Zinc" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.6 Å and deposited in 2002.

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

The PDB entry contains the structure of alpha amylase. This molecule has the UniProt identifier Q7LYT7 (Q7LYT7_PYRWO)search. The sample contained 435 residues which is 95% of the natural sequence. Out of 435 residues 435 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 Q7LYT7 (26-460) (Q7LYT7_PYRWO)search Pyrococcus woeseisearch 95% 435 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q7LYT7 (26 - 460) alpha amylase Pyrococcus woesei

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A alpha-Amylases, C-terminal beta-sheet domainsearch, Amylase, catalytic domainsearch Glycosidasessearch, Golgi alpha-mannosidase IIsearch Alpha amylase, catalytic domainsearch, Domain of unknown function (DUF1939)search

Chain ID Molecular function (GO) Biological process (GO)
A (Q7LYT7) calcium ion bindingsearch catalytic activitysearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch cation bindingsearch hydrolase activity, acting on glycosyl bondssearch metal ion bindingsearch hydrolase activitysearch alpha-amylase activitysearch carbohydrate metabolic processsearch metabolic processsearch

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