› 6tp1

X-ray diffraction
1.94Å resolution

Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with maltotetraose

Released:
DOI: 10.2210/pdb6tp1/pdb
PDB entry 6tp1 coloured by chain, front view.
PDB entry 6tp1 coloured by chain, side view.
PDB entry 6tp1 coloured by chain, top view.
Source organism: Bacillus licheniformis
Primary publication:
Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase.
Božić N, Rozeboom HJ, Lončar N, Slavić MŠ, Janssen DB, Vujčić Z
Int J Biol Macromol 165 1529-1539 (2020)
PMID: 33058974

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-516045 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Glycosyl hydrolase family 13 catalytic domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 483 amino acids
Theoretical weight: 55.31 KDa
Source organism: Bacillus licheniformis
Expression system: Escherichia coli
UniProt:
  • Canonical: I3P686 (Residues: 1-483; Coverage: 100%)
Gene name: amy
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
4 bound ligands:
Ligand CA 2 x CA
Ligand NA 2 x NA
Ligand MLI 1 x MLI
Ligand ACY 2 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P43212
Unit cell:
a: 82.08Å b: 82.08Å c: 186.34Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.201
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Which Extraction Solvents and Methods Are More Effective in Terms of Chemical Composition and Biological Activity of Alceafasciculiflora from Turkey?
Ozturk et al. (2022)
2 other articles

1 mention without citation

Native to designed: microbial -amylases for industrial applications.
Lim et al. (2021)