5JIW
Crystal structure of Thermus aquaticus amylomaltase (GH77) in complex with a 34-meric cycloamylose
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | 4-alpha-glucanotransferase | polymer | 500 | 57229.0 | 1 | UniProt (O87172) | Thermus aquaticus | Amylomaltase,Disproportionating enzyme,D-enzyme |
| 2 | B (B) | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose | branched | 2774.4 | 1 | In PDB GlyTouCan (G01206BC) | |||
| 3 | C, D (A) | 1,2-ETHANEDIOL | non-polymer | 62.1 | 2 | Chemie (EDO) | |||
| 4 | E (A) | CARBONATE ION | non-polymer | 60.0 | 1 | Chemie (CO3) | |||
| 5 | F (A) | water | water | 18.0 | 443 | Chemie (HOH) |
Sequence modifications
A: 1 - 500 (UniProt: O87172)
| PDB | External Database | Details |
|---|---|---|
| Ala 293 | Asp 293 | engineered mutation |
| Snn 370 | Asp 370 | conflict |
| Asn 395 | Asp 395 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 57229.0 | |
| Branched | Number of molecules | 1 |
| Total formula weight | 2774.4 | |
| Non-Polymers* | Number of molecules | 3 |
| Total formula weight | 184.1 | |
| All* | Total formula weight | 60187.6 |
