PDBe 1rp8

X-ray diffraction
2Å resolution

Crystal structure of barley alpha-amylase isozyme 1 (amy1) inactive mutant d180a in complex with maltoheptaose

Released:
Source organism: Hordeum vulgare
Primary publication:
Oligosaccharide binding to barley alpha-amylase 1.
J. Biol. Chem. 280 32968-78 (2005)
PMID: 16030022

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-amylase type A isozyme Chain: A
Molecule details ›
Chain: A
Length: 405 amino acids
Theoretical weight: 44.6 KDa
Source organism: Hordeum vulgare
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P00693 (Residues: 25-429; Coverage: 98%)
Gene name: AMY1.1
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21212
Unit cell:
a: 93Å b: 72.5Å c: 62.18Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.172 0.221
Expression system: Komagataella pastoris