› 1z32

X-ray diffraction
1.6Å resolution

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

Released:
DOI: 10.2210/pdb1z32/pdb
PDB entry 1z32 coloured by chain, front view.
PDB entry 1z32 coloured by chain, side view.
PDB entry 1z32 coloured by chain, top view.
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:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145124 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-amylase 1A 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: P0DUB6 (Residues: 16-511; Coverage: 100%)
Gene names: AMY1, AMY1A
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand GLC 1 x GLC
Ligand AGL 1 x AGL
Ligand HMC 1 x HMC
Ligand CA 1 x CA
Ligand CL 1 x CL
1 modified residue:
Ligand PCA 1 x PCA

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

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