› 1kxh

X-ray diffraction
2.3Å resolution

Crystal structure of the complex between an inactive mutant of psychrophilic alpha-amylase (D174N) and acarbose

Released:
DOI: 10.2210/pdb1kxh/pdb
PDB entry 1kxh coloured by chain, front view.
PDB entry 1kxh coloured by chain, side view.
PDB entry 1kxh coloured by chain, top view.
Source organism: Pseudoalteromonas haloplanktis
Primary publication:
Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic alpha-amylase.
Aghajari N, Roth M, Haser R
Biochemistry 41 4273-80 (2002)
PMID: 11914073

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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151585 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 448 amino acids
Theoretical weight: 48.95 KDa
Source organism: Pseudoalteromonas haloplanktis
Expression system: Escherichia coli
UniProt:
  • Canonical: P29957 (Residues: 25-472; Coverage: 70%)
Gene name: amy
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, AC1
Ligand GLC 2 x GLC
Ligand AC1 1 x AC1
2 bound ligands:
Ligand CA 1 x CA
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: C2221
Unit cell:
a: 71.1Å b: 139.9Å c: 115.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.138 0.138 0.188
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Psychrophilic enzymes: from folding to function and biotechnology.
Feller G. (2013)
4 more

1 mention without citation

Metabolomics-based profiling of 4 avocado varieties using HPLC-MS/MS and GC/MS and evaluation of their antidiabetic activity.
Younis et al. (2022)