PDBe 3ij7

X-ray diffraction
2Å resolution

Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase

Released:

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pancreatic alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 496 amino acids
Theoretical weight: 55.93 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P04746 (Residues: 17-511; Coverage: 100%)
Gene name: AMY2A
Sequence domains:
Structure domains:

Ligands and Environments


1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 52.14Å b: 67.82Å c: 129.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 0.229
Expression system: Komagataella pastoris