1Q4N
Structural studies of Phe256Trp of human salivary alpha-amylase: implications for the role of a conserved water molecule and its associated chain in enzyme activity
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (X) | Alpha-amylase, salivary | polymer | 496 | 55994.3 | 1 | UniProt (P04745) Pfam (PF00128) Pfam (PF02806) UniProt (by SIFTS) (P0DUB6) | Homo sapiens (human) | 1,4-alpha-D-glucan glucanohydrolase |
| 2 | B (X) | CALCIUM ION | non-polymer | 40.1 | 1 | Chemie (CA) | |||
| 3 | C (X) | CHLORIDE ION | non-polymer | 35.5 | 1 | Chemie (CL) | |||
| 4 | D (X) | TRIS(HYDROXYETHYL)AMINOMETHANE | non-polymer | 163.2 | 1 | Chemie (TAM) | |||
| 5 | E (X) | water | water | 18.0 | 324 | Chemie (HOH) |
Sequence modifications
X: 1 - 496 (UniProt: P04745)
| PDB | External Database | Details |
|---|---|---|
| Trp 256 | Phe 271 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 55994.3 | |
| Non-Polymers* | Number of molecules | 3 |
| Total formula weight | 238.7 | |
| All* | Total formula weight | 56233.0 |
