› 8orp

X-ray diffraction
2Å resolution

Crystal structure of Drosophila melanogaster alpha-amylase in complex with the inhibitor acarbose

Released:
DOI: 10.2210/pdb8orp/pdb
PDB entry 8orp coloured by chain, front view.
PDB entry 8orp coloured by chain, side view.
PDB entry 8orp coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
Structural and Functional Characterization of Drosophila melanogaster α-Amylase.
Rhimi M, Da Lage JL, Haser R, Feller G, Aghajari N
Molecules 28 (2023)
PMID: 37513201

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-225088 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Alpha-amylase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 494 amino acids
Theoretical weight: 53.8 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia
UniProt:
  • Canonical: P08144 (Residues: 1-494; Coverage: 100%)
Gene names: Amy-p, AmyA, CG18730
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GLC, RY7
Ligand BGC 2 x BGC
Ligand GLC 2 x GLC
Ligand RY7 2 x RY7
Carbohydrate polymer : NEW Components: GLC, RY7
Ligand GLC 2 x GLC
Ligand RY7 2 x RY7
3 bound ligands:
Ligand CL 2 x CL
Ligand EDO 38 x EDO
Ligand SR 4 x SR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 80.08Å b: 72.54Å c: 98.21Å
α: 90° β: 98.41° γ: 90°
R-values:
R R work R free
0.176 0.174 0.212
Expression system: Escherichia

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Citations

2 review citations

Analyzing Current Trends and Possible Strategies to Improve Sucrose Isomerases' Thermostability.
Sardiña-Peña et al. (2023)
1 more