› 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:
DOI: 10.2210/pdb1q4n/pdb
PDB entry 1q4n coloured by chain, front view.
PDB entry 1q4n coloured by chain, side view.
PDB entry 1q4n coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural studies of a Phe256Trp mutant of human salivary alpha-amylase: implications for the role of a conserved water molecule in enzyme activity.
Ramasubbu N, Sundar K, Ragunath C, Rafi MM
Arch Biochem Biophys 421 115-24 (2004)
PMID: 14678792

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: 55.99 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

3 bound ligands:
Ligand CA 1 x CA
Ligand CL 1 x CL
Ligand TAM 1 x TAM
1 modified residue:
Ligand PCA 1 x PCA

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

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Citations

2 review citations

Phytotherapy in diabetes: Review on potential mechanistic perspectives.
El-Abhar et al. (2014)
1 more