› 1jfh

X-ray diffraction
2.03Å resolution

STRUCTURE OF A PANCREATIC ALPHA-AMYLASE BOUND TO A SUBSTRATE ANALOGUE AT 2.03 ANGSTROM RESOLUTION

Released:
DOI: 10.2210/pdb1jfh/pdb
PDB entry 1jfh coloured by chain, front view.
PDB entry 1jfh coloured by chain, side view.
PDB entry 1jfh coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03 A resolution.
Qian M, Spinelli S, Driguez H, Payan F
Protein Sci 6 2285-96 (1997)
PMID: 9385631

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-132822 (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: 55.43 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P00690 (Residues: 16-511; Coverage: 100%)
Gene name: AMY2
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: MA3, MA2
Ligand MA3 1 x MA3
Ligand MA2 1 x MA2
Carbohydrate polymer : NEW Components: MA1, GLC
Ligand MA1 2 x MA1
Ligand GLC 2 x GLC
3 bound ligands:
Ligand CL 1 x CL
Ligand HG 1 x HG
Ligand CA 1 x CA
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 56.3Å b: 87.8Å c: 103.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.16 0.185

Quick links

Citations

3 review citations

Recognition between flexible protein molecules: induced and assisted folding.
Demchenko AP. (2001)
2 more

2 mentions without citation

Defining structural and evolutionary modules in proteins: a community detection approach to explore sub-domain architecture.
Hleap et al. (2013)
1 more