› 5u3a

X-ray diffraction
0.95Å resolution

Ultra High Resolution Crystal Structure of Human Pancreatic Alpha Amylase

Released:
DOI: 10.2210/pdb5u3a/pdb
PDB entry 5u3a coloured by chain, front view.
PDB entry 5u3a coloured by chain, side view.
PDB entry 5u3a coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Folding Then Binding vs Folding Through Binding in Macrocyclic Peptide Inhibitors of Human Pancreatic α-Amylase.
Goldbach L, Vermeulen BJA, Caner S, Liu M, Tysoe C, van Gijzel L, Yoshisada R, Trellet M, van Ingen H, Brayer GD, Bonvin AMJJ, Jongkees SAK
ACS Chem Biol 14 1751-1759 (2019)
PMID: 31241898

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 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: 55.93 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P212121
Unit cell:
a: 52.1Å b: 67.84Å c: 130.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.11 0.11 0.12
Expression system: Komagataella pastoris

Quick links

Citations

1 review citation

Peptide Folding and Binding Probed by Systematic Non-canonical Mutagenesis.
Rogers JM. (2020)
4 other articles

10 mentions without citation

Enhancing glycan stability via site-selective fluorination: modulating substrate orientation by molecular design.
Axer et al. (2020)
9 more