› 2aaa

X-ray diffraction
2.12Å resolution

CALCIUM BINDING IN ALPHA-AMYLASES: AN X-RAY DIFFRACTION STUDY AT 2.1 ANGSTROMS RESOLUTION OF TWO ENZYMES FROM ASPERGILLUS

Released:
DOI: 10.2210/pdb2aaa/pdb
PDB entry 2aaa coloured by chain, front view.
PDB entry 2aaa coloured by chain, side view.
PDB entry 2aaa coloured by chain, top view.
Source organism: Aspergillus niger
Primary publication:
Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus.
Boel E, Brady L, Brzozowski AM, Derewenda Z, Dodson GG, Jensen VJ, Petersen SB, Swift H, Thim L, Woldike HF
Biochemistry 29 6244-9 (1990)
PMID: 2207069

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:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157447 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acid alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 484 amino acids
Theoretical weight: 52.97 KDa
Source organism: Aspergillus niger
Expression system: Not provided
UniProt:
  • Canonical: P56271 (Residues: 1-484; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 81.1Å b: 98.3Å c: 138Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 not available not available
Expression system: Not provided

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Citations

16 review citations

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
Vieille et al. (2001)
15 more

30 mentions without citation

Role of the retinal vascular endothelial cell in ocular disease.
Bharadwaj et al. (2013)
29 more