› 1mwo

X-ray diffraction
2.2Å resolution

Crystal Structure Analysis of the Hyperthermostable Pyrocoocus woesei alpha-amylase

Released:
DOI: 10.2210/pdb1mwo/pdb
PDB entry 1mwo coloured by chain, front view.
PDB entry 1mwo coloured by chain, side view.
PDB entry 1mwo coloured by chain, top view.
Source organism: Pyrococcus woesei
Primary publication:
Differential regulation of a hyperthermophilic alpha-amylase with a novel (Ca,Zn) two-metal center by zinc.
Linden A, Mayans O, Meyer-Klaucke W, Antranikian G, Wilmanns M
J Biol Chem 278 9875-84 (2003)
PMID: 12482867

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-181678 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycosyl hydrolase family 13 catalytic domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 435 amino acids
Theoretical weight: 50.23 KDa
Source organism: Pyrococcus woesei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7LYT7 (Residues: 26-460; Coverage: 95%)
Gene name: amyA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 6 x ZN
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 62.88Å b: 78.2Å c: 106.289Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.224
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

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

2 mentions without citation

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