› 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:
DOI: 10.2210/pdb3ij7/pdb
PDB entry 3ij7 coloured by chain, front view.
PDB entry 3ij7 coloured by chain, side view.
PDB entry 3ij7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Directed "in situ" inhibitor elongation as a strategy to structurally characterize the covalent glycosyl-enzyme intermediate of human pancreatic alpha-amylase.
Zhang R, Li C, Williams LK, Rempel BP, Brayer GD, Withers SG
Biochemistry 48 10752-64 (2009)
PMID: 19803533

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
Macromolecules (3 distinct):
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

Carbohydrate polymer : NEW Components: B9D, BGC, B8D
Carbohydrate polymer
Carbohydrate polymer : NEW Components: B8D, GLF
Carbohydrate polymer
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: 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

Quick links

Citations

15 citation in other articles

Structures of human pancreatic α-amylase in complex with acarviostatins: Implications for drug design against type II diabetes.
Qin et al. (2011)
14 more