PDBe 1xv8

X-ray diffraction
3Å resolution

Crystal Structure of Human Salivary Alpha-Amylase Dimer

Released:
Source organism: Homo sapiens
Entry authors: Fisher SZ, Govindasamy L, Tu CK, Silverman DN, Rajaniemi H, McKenna R

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-amylase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 496 amino acids
Theoretical weight: 55.96 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P04745 (Residues: 16-511; Coverage: 100%)
Gene names: AMY1, AMY1A, AMY1B, AMY1C
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 150.812Å b: 72.27Å c: 91.106Å
α: 90° β: 102.8° γ: 90°
R-values:
R R work R free
0.228 0.228 0.271