1UD3
Crystal structure of AmyK38 N289H mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004556 | molecular_function | alpha-amylase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 1001 |
| Chain | Residue |
| A | ASN104 |
| A | ASP194 |
| A | ASN200 |
| A | HIS235 |
| A | HOH2032 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 1002 |
| Chain | Residue |
| A | ASN427 |
| A | HOH2182 |
| A | GLY300 |
| A | TYR302 |
| A | TRP403 |
| A | ASP404 |
