3blk Summary

pdbe.org/3blk
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Role of aromatic residues in starch binding

The structure was published by Ragunath, C., Manuel, S.G.A., Kasinathan, C., and Ramasubbu, N., in 2008 in a paper entitled "Structure-function relationships in human salivary alpha-amylase: role of aromatic residues in a secondary binding site" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2007.

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

The PDB entry contains the structure of Alpha-amylase 1. This molecule has the UniProt identifier P04745 (AMY1_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 1 P04745 (16-511) (AMY1_HUMAN)search Homo sapienssearch 99% 496 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P04745 (16 - 511) Alpha-amylase 1 Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A (P04745) 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 (P04745) carbohydrate metabolic processsearch metabolic processsearch digestionsearch cation bindingsearch catalytic activitysearch protein bindingsearch metal ion bindingsearch hydrolase activity, acting on glycosyl bondssearch alpha-amylase activitysearch hydrolase activitysearch extracellular regionsearch extracellular spacesearch extracellular vesicular exosomesearch

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