› 1kbb

X-ray diffraction
1.9Å resolution

Mechanistic Analyses of Catalysis in Human Pancreatic alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids

Released:
DOI: 10.2210/pdb1kbb/pdb
PDB entry 1kbb coloured by chain, front view.
PDB entry 1kbb coloured by chain, side view.
PDB entry 1kbb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids.
Rydberg EH, Li C, Maurus R, Overall CM, Brayer GD, Withers SG
Biochemistry 41 4492-502 (2002)
PMID: 11914097

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-138163 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pancreatic alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 496 amino acids
Theoretical weight: 55.87 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P04746 (Residues: 16-511; Coverage: 100%)
Gene name: AMY2A
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 RU300
Spacegroup: P212121
Unit cell:
a: 52.92Å b: 74.77Å c: 136.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.172 0.194
Expression system: Komagataella pastoris

Quick links

Citations

2 review citations

The alpha-L-fucosidase from Sulfolobus solfataricus.
Cobucci-Ponzano et al. (2008)
1 more

1 mention without citation

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