› 1jxk

X-ray diffraction
1.9Å resolution

Role of ethe mobile loop in the mehanism of human salivary amylase

Released:
DOI: 10.2210/pdb1jxk/pdb
PDB entry 1jxk coloured by chain, front view.
PDB entry 1jxk coloured by chain, side view.
PDB entry 1jxk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase.
Ramasubbu N, Ragunath C, Mishra PJ
J Mol Biol 325 1061-76 (2003)
PMID: 12527308

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: A
Molecule details ›
Chain: A
Length: 491 amino acids
Theoretical weight: 55.64 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P0DUB6 (Residues: 16-511; Coverage: 99%)
Gene names: AMY1, AMY1A
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
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: RIGAKU
Spacegroup: P212121
Unit cell:
a: 52.9Å b: 75.737Å c: 134.554Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.173 0.2
Expression system: Spodoptera frugiperda

Quick links

Citations

2 review citations

α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.
Janeček et al. (2014)
1 more

1 mention without citation

Structure of human salivary alpha-amylase crystallized in a C-centered monoclinic space group.
Fisher et al. (2006)