1KBB
Mechanistic Analyses of Catalysis in Human Pancreatic alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A (A) | ALPHA-AMYLASE, PANCREATIC | polymer | 496 | 55873.3 | 1 | UniProt (P04746) Pfam (PF00128) Pfam (PF02806) | Homo sapiens (human) | 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE, PANCREATIC ALPHA-AMYLASE |
2 | B (A) | CALCIUM ION | non-polymer | 40.1 | 1 | Chemie (CA) | |||
3 | C (A) | CHLORIDE ION | non-polymer | 35.5 | 1 | Chemie (CL) | |||
4 | D (A) | water | water | 18.0 | 120 | Chemie (HOH) |
Sequence modifications
A: 1 - 496 (UniProt: P04746)
PDB | External Database | Details |
---|---|---|
Ala 233 | Glu 248 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 1 |
Total formula weight | 55873.3 | |
Non-Polymers* | Number of molecules | 2 |
Total formula weight | 75.5 | |
All* | Total formula weight | 55948.8 |