1xcw Summary

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Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts

The structure was published by Li, C., Begum, A., Numao, S., Park, K.H., Withers, S.G., and Brayer, G.D., in 2005 in a paper entitled "Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 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. 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 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) 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 Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P04746) carbohydrate metabolic processsearch metabolic processsearch small molecule metabolic processsearch polysaccharide digestionsearch carbohydrate catabolic processsearch hydrolase activitysearch cation bindingsearch catalytic activitysearch metal ion bindingsearch calcium ion bindingsearch alpha-amylase activitysearch chloride ion bindingsearch hydrolase activity, acting on glycosyl bondssearch extracellular vesicular exosomesearch extracellular spacesearch extracellular regionsearch

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