2qv4 Summary


Human pancreatic alpha-amylase complexed with nitrite and acarbose

The structure was published by Maurus, R., Begum, A., Williams, L.K., et al., Zhang, R., Withers, S.G., and Brayer, G.D., in 2008 in a paper entitled "Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.97 Å and deposited in 2007.

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

The PDB entry contains the structure of Pancreatic alpha-amylase. This molecule has the UniProt identifier P04746 (AMYP_HUMAN)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 Pancreatic alpha-amylase P04746 (16-511) (AMYP_HUMAN)search Homo sapienssearch 100% 496 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P04746 (16 - 511) Pancreatic alpha-amylase Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P04746) 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 Cellular component (GO) Biological process (GO) Molecular function (GO)
A (P04746) extracellular regionsearch extracellular spacesearch carbohydrate catabolic processsearch carbohydrate metabolic processsearch metabolic processsearch small molecule metabolic processsearch polysaccharide digestionsearch catalytic activitysearch cation bindingsearch calcium ion bindingsearch alpha-amylase activitysearch hydrolase activitysearch metal ion bindingsearch hydrolase activity, acting on glycosyl bondssearch chloride ion bindingsearch

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