1vep Summary

pdbe.org/1vep
spacer

Crystal Structure Analysis of Triple (T47M/Y164E/T328N)/maltose of Bacillus cereus Beta-Amylase at pH 6.5

The structure was published by Hirata, A., Adachi, M., Utsumi, S., and Mikami, B., in 2004 in a paper entitled "Engineering of the pH optimum of Bacillus cereus beta-amylase: conversion of the pH optimum from a bacterial type to a higher-plant type" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.06 Å and deposited in 2004.

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 P36924 (AMYB_BACCE)search. The sample contained 516 residues which is 100% of the natural sequence. Out of 516 residues 516 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 P36924 (31-546) (AMYB_BACCE)search Bacillus cereussearch 100% 516 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P36924 (31 - 546) Beta-amylase Bacillus cereus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P36924) Starch-binding domainsearch, Amylase, catalytic domainsearch Glycosidasessearch, Immunoglobulinssearch PF00686: Starch binding domainsearch, PF01373: Glycosyl hydrolase family 14search

Chain ID Molecular function (GO) Biological process (GO)
A (P36924) starch bindingsearch beta-amylase activitysearch hydrolase activitysearch metal ion bindingsearch hydrolase activity, acting on glycosyl bondssearch polysaccharide metabolic processsearch polysaccharide catabolic processsearch carbohydrate metabolic processsearch metabolic processsearch

Chain InterPro annotation
A Glycoside hydrolase, family 14A, bacterialsearch Glycoside hydrolase, family 14search Carbohydrate binding module family 20search Glycoside hydrolase, catalytic domainsearch Immunoglobulin-like foldsearch Glycoside hydrolase superfamilysearch Glycoside hydrolase, family 14, conserved sitesearch