3IJ8
Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A | Pancreatic alpha-amylase | polymer | 496 | 55931.3 | 1 | UniProt (P04746) Pfam (PF00128) Pfam (PF02806) In PDB | Homo sapiens (human) | PA, 1,4-alpha-D-glucan glucanohydrolase |
2 | A | (2R,3S,4R,5R,6R)-2,6-difluoro-2-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol | non-polymer | 200.1 | 3 | Chemie (B0D) | |||
3 | A | 5-fluoro-alpha-L-idopyranose | non-polymer | 198.1 | 1 | Chemie (B9D) | |||
4 | A | CALCIUM ION | non-polymer | 40.1 | 1 | Chemie (CA) | |||
5 | A | CHLORIDE ION | non-polymer | 35.5 | 1 | Chemie (CL) | |||
6 | water | water | 18.0 | 405 | Chemie (HOH) |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 1 |
Total formula weight | 55931.3 | |
Non-Polymers* | Number of molecules | 6 |
Total formula weight | 874.1 | |
All* | Total formula weight | 56805.4 |