› 1qpk

X-ray diffraction
2Å resolution

MUTANT (D193G) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH MALTOTETRAOSE

Released:
DOI: 10.2210/pdb1qpk/pdb
PDB entry 1qpk coloured by chain, front view.
PDB entry 1qpk coloured by chain, side view.
PDB entry 1qpk coloured by chain, top view.
Source organism: Pseudomonas stutzeri
Primary publication:
Roles of catalytic residues in alpha-amylases as evidenced by the structures of the product-complexed mutants of a maltotetraose-forming amylase.
Hasegawa K, Kubota M, Matsuura Y
Protein Eng 12 819-24 (1999)
PMID: 10556241

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146628 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Glucan 1,4-alpha-maltotetraohydrolase Chain: A
Molecule details ›
Chain: A
Length: 418 amino acids
Theoretical weight: 46.52 KDa
Source organism: Pseudomonas stutzeri
Expression system: Escherichia coli
UniProt:
  • Canonical: P13507 (Residues: 22-439; Coverage: 79%)
Gene name: amyP
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 63.21Å b: 167.5Å c: 46.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 not available not available
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Engineering yeasts for raw starch conversion.
van Zyl et al. (2012)
2 more

1 mention without citation

D-arginine Enhances the Effect of Alpha-Amylase on Disassembling Actinomyces viscosus Biofilm.
Li et al. (2022)