› 3blp

X-ray diffraction
1.6Å resolution

Role of aromatic residues in human salivary alpha-amylase

Released:
DOI: 10.2210/pdb3blp/pdb
PDB entry 3blp coloured by chain, front view.
PDB entry 3blp coloured by chain, side view.
PDB entry 3blp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-function relationships in human salivary alpha-amylase: role of aromatic residues in a secondary binding site
Ragunath C, Kasinathan C, Manuel SGA, Ramasubbu N
Biologia 63 1028-1034 (2008)

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145124 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Alpha-amylase 1A Chain: X
Molecule details ›
Chain: X
Length: 496 amino acids
Theoretical weight: 55.84 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P0DUB6 (Residues: 16-511; Coverage: 100%)
Gene names: AMY1, AMY1A
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, AGL
Carbohydrate polymer
3 bound ligands:
Ligand CA 1 x CA
Ligand CL 1 x CL
Ligand HMC 1 x HMC
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P212121
Unit cell:
a: 52.085Å b: 74.873Å c: 134.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.181 0.205
Expression system: Spodoptera frugiperda

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