1u33 Summary


In situ extension as an approach for identifying novel alpha-amylase inhibitors

The structure was published by Numao, S., Damager, I., Li, C., et al., Overall, C.M., Brayer, G.D., and Withers, S.G., in 2004 in a paper entitled "In Situ Extension as an Approach for Identifying Novel alpha-Amylase Inhibitors." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.95 Å and deposited in 2004.

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

The PDB entry contains the structure of Alpha-amylase, pancreatic. 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 495 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, pancreatic 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) Alpha-amylase, pancreatic 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 Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P04746) alpha-amylase activitysearch hydrolase activity, acting on glycosyl bondssearch hydrolase activitysearch catalytic activitysearch cation bindingsearch chloride ion bindingsearch calcium ion bindingsearch metal ion bindingsearch extracellular spacesearch extracellular regionsearch carbohydrate metabolic processsearch metabolic processsearch polysaccharide digestionsearch small molecule metabolic processsearch carbohydrate catabolic processsearch

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