PDBe 1z32

X-ray diffraction
1.6Å resolution

Structure-function relationships in human salivary alpha-amylase: Role of aromatic residues

Released:
Source organism: Homo sapiens
Entry authors: Ramasubbu N, Ragunath C, Sundar K, Mishra PJ, Gyemant G, Kandra L

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: 55.92 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


1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P212121
Unit cell:
a: 51.657Å b: 73.513Å c: 134.362Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.171 0.192
Expression system: Spodoptera frugiperda