2xfr Summary

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Crystal structure of barley beta-amylase at atomic resolution

The structure was published by Rejzek, M., Stevenson, C.E.M., Southard, A.M., et al., Naldrett, M.J., Lawson, D.M., and Field, R.A., in 2011 in a paper entitled "Chemical Genetics and Cereal Starch Metabolism: Structural Basis of the Non-Covalent and Covalent Inhibition of Barley Beta-Amylase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 0.97 Å and deposited in 2010.

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

The PDB entry contains the structure of BETA-AMYLASE. This molecule has the UniProt identifier P16098 (AMYB_HORVU)search. The sample contained 535 residues which is 100% of the natural sequence. Out of 535 residues 486 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 BETA-AMYLASE P16098 (1-535) (AMYB_HORVU)search Hordeum vulgaresearch 93% 535 91%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P16098 (1 - 535) BETA-AMYLASE Hordeum vulgare

Chain Structural classification (CATH) Sequence family (Pfam)
A (P16098) Glycosidasessearch PF01373: Glycosyl hydrolase family 14search

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

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