1AJC
THREE-DIMENSIONAL STRUCTURE OF THE D153G MUTANT OF E. COLI ALKALINE PHOSPHATASE: A MUTANT WITH WEAKER MAGNESIUM BINDING AND INCREASED CATALYTIC ACTIVITY
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B | ALKALINE PHOSPHATASE | polymer | 449 | 47037.3 | 2 | UniProt (P00634) Pfam (PF00245) In PDB | Escherichia coli | |
| 2 | A, B | ZINC ION | non-polymer | 65.4 | 4 | Chemie (ZN) | |||
| 3 | A, B | MAGNESIUM ION | non-polymer | 24.3 | 2 | Chemie (MG) | |||
| 4 | water | water | 18.0 | 3 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 449 (UniProt: P00634)
| PDB | External Database | Details |
|---|---|---|
| Gly 153 | Asp 175 | engineered mutation |
| Glu 230 | Gln 252 | conflict |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 94074.7 | |
| Non-Polymers* | Number of molecules | 6 |
| Total formula weight | 310.2 | |
| All* | Total formula weight | 94384.9 |
