› 1ven

X-ray diffraction
2.02Å resolution

Crystal Structure Analysis of Y164E/maltose of Bacilus cereus Beta-amylase at pH 4.6

Released:
DOI: 10.2210/pdb1ven/pdb
PDB entry 1ven coloured by chain, front view.
PDB entry 1ven coloured by chain, side view.
PDB entry 1ven coloured by chain, top view.
Source organism: Bacillus cereus
Primary publication:
Engineering of the pH optimum of Bacillus cereus beta-amylase: conversion of the pH optimum from a bacterial type to a higher-plant type.
Hirata A, Adachi M, Utsumi S, Mikami B
Biochemistry 43 12523-31 (2004)
PMID: 15449941

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-amylase Chain: A
Molecule details ›
Chain: A
Length: 516 amino acids
Theoretical weight: 58.32 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli
UniProt:
  • Canonical: P36924 (Residues: 31-546; Coverage: 100%)
Gene name: spoII
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GLC 2 x GLC
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P21
Unit cell:
a: 57.489Å b: 92.899Å c: 65.962Å
α: 90° β: 102.36° γ: 90°
R-values:
R R work R free
0.193 0.193 0.229
Expression system: Escherichia coli

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Citations

12 citation in other articles

Redesigning protein pKa values.
Tynan-Connolly et al. (2007)
11 more

1 mention without citation

Phytochemical and antimicrobial investigation of the leaves of five Egyptian mango cultivars and evaluation of their essential oils as preservatives materials.
Ouf et al. (2021)