3eqa Summary


Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol

The structure was published by Lee, J. and Paetzel, M., in 2011 in a paper entitled "Structure of the catalytic domain of glucoamylase from Aspergillus niger." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2008.

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

The PDB entry contains the structure of Glucoamylase. This molecule has the UniProt identifier P69328 (AMYG_ASPNG)search. The sample contained 470 residues which is < 90% of the natural sequence. Out of 470 residues 458 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 Glucoamylase P69328 (25-494) (AMYG_ASPNG)search Aspergillus nigersearch < 90% 470 97%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P69328 (25 - 494) Glucoamylase Aspergillus niger

Chain Structural classification (CATH) Sequence family (Pfam)
A Glycosyltransferasesearch Glycosyl hydrolases family 15search

Chain ID Biological process (GO) Molecular function (GO)
A (P69328) polysaccharide metabolic processsearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch glucan 1,4-alpha-glucosidase activitysearch catalytic activitysearch

Chain InterPro annotation
A Glucoamylasesearch Six-hairpin glycosidase-likesearch Glycoside hydrolase family 15search Six-hairpin glycosidasesearch