1tmq Summary



The structure was published by Strobl, S., Maskos, K., Wiegand, G., Huber, R., Gomis-Ruth, F.X., and Glockshuber, R., in 1998 in a paper entitled "A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1998.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely PROTEIN (ALPHA-AMYLASE) and PROTEIN (RAGI BIFUNCTIONAL INHIBITOR).

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 most likely forms heterodimers.

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 PROTEIN (ALPHA-AMYLASE) P56634 (1-471) (AMY_TENMO)search Tenebrio molitorsearch 100% 471 100%
B PROTEIN (RAGI BIFUNCTIONAL INHIBITOR) P01087 (1-117) (IAAT_ELECO)search Eleusine coracanasearch 96% 117 100%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P56634 (1 - 471) PROTEIN (ALPHA-AMYLASE) Tenebrio molitor
P01087 (1 - 117) PROTEIN (RAGI BIFUNCTIONAL INHIBITOR) Eleusine coracana

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P56634) 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
B (P01087) Proteinase/alpha-amylase inhibitorssearch Plant lipid-transfer and hydrophobic proteinssearch PF00234: Protease inhibitor/seed storage/LTP familysearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P56634) cation bindingsearch catalytic activitysearch alpha-amylase activitysearch hydrolase activity, acting on glycosyl bondssearch hydrolase activitysearch metal ion bindingsearch carbohydrate metabolic processsearch metabolic processsearch
B (P01087) serine-type endopeptidase inhibitor activitysearch peptidase inhibitor activitysearch alpha-amylase inhibitor activitysearch negative regulation of peptidase activitysearch negative regulation of endopeptidase activitysearch 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
B Cereal seed allergen/trypsin and alpha-amylase inhibitor, conserved sitesearch Cereal seed allergen/grain softness/trypsin and alpha-amylase inhibitorsearch Bifunctional trypsin/alpha-amylase inhibitor helical domainsearch Bifunctional inhibitor/plant lipid transfer protein/seed storage helical domainsearch