2aaa Summary

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CALCIUM BINDING IN ALPHA-AMYLASES: AN X-RAY DIFFRACTION STUDY AT 2.1 ANGSTROMS RESOLUTION OF TWO ENZYMES FROM ASPERGILLUS

The structure was published by Boel, E., Brady, L., Brzozowski, A.M., et al., Swift, H., Thim, L., and Woldike, H.F., in 1990 in a paper entitled "Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.12 Å and deposited in 1991.

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 P56271 (AMYA_ASPNG)search. The sample contained 484 residues which is 100% of the natural sequence. Out of 484 residues 476 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 P56271 (1-484) (AMYA_ASPNG)search Aspergillus nigersearch 100% 484 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P56271 (1 - 484) ALPHA-AMYLASE Aspergillus niger

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P56271) alpha-Amylases, C-terminal beta-sheet domainsearch, Amylase, catalytic domainsearch Glycosidasessearch, Golgi alpha-mannosidase IIsearch PF00128: Alpha amylase, catalytic domainsearch, PF09260: Domain of unknown function (DUF1966)search

Chain ID Molecular function (GO) Biological process (GO)
A (P56271) alpha-amylase activitysearch metal ion bindingsearch catalytic activitysearch cation bindingsearch calcium ion bindingsearch hydrolase activity, acting on glycosyl bondssearch hydrolase activitysearch carbohydrate metabolic processsearch carbohydrate catabolic processsearch metabolic processsearch

Chain InterPro annotation
A Glycosyl hydrolase, family 13, catalytic domainsearch Glycosyl hydrolase, family 13, subfamily, catalytic domainsearch Alpha-amylase, fungisearch Glycosyl hydrolase, family 13, all-betasearch Glycoside hydrolase, catalytic domainsearch Alpha-amylase, domain of unknown function DUF1966, C-terminalsearch Glycoside hydrolase, family 13search Glycoside hydrolase superfamilysearch