PDBe 1q4n

X-ray diffraction
2.07Å resolution

Structural studies of Phe256Trp of human salivary alpha-amylase: implications for the role of a conserved water molecule and its associated chain in enzyme activity

Released:

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 1 Chain: X
Molecule details ›
Chain: X
Length: 496 amino acids
Theoretical weight: 55.99 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P04745 (Residues: 16-511; Coverage: 100%)
Gene names: AMY1, AMY1A, AMY1B, AMY1C
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 51.9Å b: 74.2Å c: 134.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.156 0.206
Expression system: Spodoptera frugiperda