1b1y Summary

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SEVENFOLD MUTANT OF BARLEY BETA-AMYLASE

The structure was published by Mikami, B., Yoon, H.J., and Yoshigi, N., in 1999 in a paper entitled "The crystal structure of the sevenfold mutant of barley beta-amylase with increased thermostability 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.

The PDB entry contains the structure of PROTEIN (BETA-AMYLASE). This molecule has the UniProt identifier P16098 (AMYB_HORVU)search. The sample contained 500 residues which is 93% of the natural sequence. Out of 500 residues 500 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 PROTEIN (BETA-AMYLASE) P16098 (6-504) (AMYB_HORVU)search Hordeum vulgaresearch 93% 500 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P16098 (6 - 504) PROTEIN (BETA-AMYLASE) Hordeum vulgare

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P16098) Amylase, catalytic domainsearch Glycosidasessearch PF01373: Glycosyl hydrolase family 14search

Chain ID Molecular function (GO) Biological process (GO)
A (P16098) identical protein bindingsearch beta-amylase activitysearch hydrolase activitysearch hydrolase activity, acting on glycosyl bondssearch carbohydrate metabolic processsearch polysaccharide catabolic processsearch metabolic processsearch

Chain InterPro annotation
A Glycoside hydrolase, family 14B, plantsearch Glycoside hydrolase, family 14search Glycoside hydrolase, catalytic domainsearch Glycoside hydrolase superfamilysearch Glycoside hydrolase, family 14, conserved sitesearch