› 1mxg

X-ray diffraction
1.6Å resolution

Crystal Structure of a (Ca,Zn)-dependent alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei in complex with acarbose

Released:
DOI: 10.2210/pdb1mxg/pdb
PDB entry 1mxg coloured by chain, front view.
PDB entry 1mxg coloured by chain, side view.
PDB entry 1mxg 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
Macromolecules (2 distinct):
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

Carbohydrate polymer : NEW Components: GLC, AC1
Ligand GLC 6 x GLC
Ligand AC1 3 x AC1
6 bound ligands:
Ligand ZN 1 x ZN
Ligand CA 1 x CA
Ligand MG 3 x MG
Ligand ETE 2 x ETE
Ligand TRS 1 x TRS
Ligand EOH 4 x EOH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 51.48Å b: 76.507Å c: 136.455Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.159 0.172
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

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

3 mentions without citation

Discovering structural motifs using a structural alphabet: application to magnesium-binding sites.
Dudev et al. (2007)
2 more