› 1mfu

X-ray diffraction
2Å resolution

Probing the role of a mobile loop in human salivary amylase: Structural studies on the loop-deleted mutant

Released:
DOI: 10.2210/pdb1mfu/pdb
PDB entry 1mfu coloured by chain, front view.
PDB entry 1mfu coloured by chain, side view.
PDB entry 1mfu 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
Macromolecules (4 distinct):
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: 17-511; Coverage: 99%)
Gene names: AMY1, AMY1A
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, AGL
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC, AGL
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
4 bound ligands:
Ligand HMC 4 x HMC
Ligand GLC 1 x GLC
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: 52.074Å b: 73.815Å c: 135.787Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.16 0.201
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

3 mentions without citation

Probing the role of aromatic residues at the secondary saccharide-binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding.
Ragunath et al. (2008)
2 more