› 1wza

X-ray diffraction
1.6Å resolution

Crystal structure of alpha-amylase from H.orenii

Released:
DOI: 10.2210/pdb1wza/pdb
PDB entry 1wza coloured by chain, front view.
PDB entry 1wza coloured by chain, side view.
PDB entry 1wza coloured by chain, top view.
Source organism: Halothermothrix orenii
Primary publication:
Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition.
Sivakumar N, Li N, Tang JW, Patel BK, Swaminathan K
FEBS Lett 580 2646-52 (2006)
PMID: 16647060

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-184554 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycosyl hydrolase family 13 catalytic domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 488 amino acids
Theoretical weight: 56.75 KDa
Source organism: Halothermothrix orenii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8GPL8 (Residues: 28-515; Coverage: 100%)
Gene name: amyA
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
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P212121
Unit cell:
a: 55.126Å b: 61.658Å c: 147.625Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 0.209
Expression system: Escherichia coli

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Citations

6 review citations

α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.
Janeček et al. (2014)
5 more

10 mentions without citation

Structural and functional adaptation in extremophilic microbial α-amylases.
Ahmad et al. (2022)
9 more