3DHP
Probing the role of aromatic residues at the secondary saccharide binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding
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 1 | polymer | 496 | 55287.5 | 1 | UniProt (P04745) Pfam (PF00128) Pfam (PF02806) UniProt (by SIFTS) (P0DUB6) | Homo sapiens (human) | 1,4-alpha-D-glucan glucanohydrolase 1, Salivary alpha-amylase |
| 2 | B (B) | 4-amino-4,6-dideoxy-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose | branched | 325.3 | 1 | In PDB GlyTouCan (G90989WB) | |||
| 3 | C (A) | alpha-D-glucopyranose | non-polymer | 180.2 | 1 | Chemie (GLC) | |||
| 4 | D (A) | CALCIUM ION | non-polymer | 40.1 | 1 | Chemie (CA) | |||
| 5 | E (A) | CHLORIDE ION | non-polymer | 35.5 | 1 | Chemie (CL) | |||
| 6 | F (A) | 5-HYDROXYMETHYL-CHONDURITOL | non-polymer | 176.2 | 1 | Chemie (HMC) | |||
| 7 | G (A) | water | water | 18.0 | 444 | Chemie (HOH) |
Sequence modifications
A: 1 - 496 (UniProt: P04745)
| PDB | External Database | Details |
|---|---|---|
| Ala 134 | Trp 149 | engineered mutation |
| Ala 203 | Trp 218 | engineered mutation |
| Ala 276 | Tyr 291 | engineered mutation |
| Ala 284 | Trp 299 | engineered mutation |
| Ala 316 | Trp 331 | engineered mutation |
| Ala 388 | Trp 403 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 55287.5 | |
| Branched | Number of molecules | 1 |
| Total formula weight | 325.3 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 431.9 | |
| All* | Total formula weight | 56044.7 |
