1OB0
Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A | ALPHA-AMYLASE | polymer | 483 | 55314.0 | 1 | UniProt (P06278) Pfam (PF00128) Pfam (PF09154) In PDB | BACILLUS LICHENIFORMIS | 1,4-ALPHA-D-GLUCAN-4-GLUCANOHYDROLASE |
| 2 | A | CALCIUM ION | non-polymer | 40.1 | 3 | Chemie (CA) | |||
| 3 | A | SODIUM ION | non-polymer | 23.0 | 1 | Chemie (NA) | |||
| 4 | water | water | 18.0 | 324 | Chemie (HOH) |
Sequence modifications
A: 1 - 483 (UniProt: P06278)
| PDB | External Database | Details |
|---|---|---|
| Val 133 | His 162 | engineered mutation |
| Leu 134 | Arg 163 | conflict |
| Phe 190 | Asn 219 | engineered mutation |
| Val 209 | Ala 238 | engineered mutation |
| Ser 264 | Gln 293 | engineered mutation |
| Tyr 265 | Asn 294 | engineered mutation |
| Gly 310 | Ser 339 | conflict |
| Ser 320 | Ala 349 | conflict |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 55314.0 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 143.2 | |
| All* | Total formula weight | 55457.3 |
