1smd Summary

pdbe.org/1smd
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HUMAN SALIVARY AMYLASE

The structure was published by Ramasubbu, N., Paloth, V., Luo, Y., Brayer, G.D., and Levine, M.J., in 1996 in a paper entitled "Structure of human salivary alpha-amylase at 1.6 A resolution: implications for its role in the oral cavity." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.6 Å and deposited in 1996.

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

The PDB entry contains the structure of AMYLASE. 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 AMYLASE P04745 (17-511) (AMY1_HUMAN)search Homo sapienssearch 99% 496 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P04745 (17 - 511) AMYLASE Homo sapiens

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