1GES
ANATOMY OF AN ENGINEERED NAD-BINDING SITE
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B (A, B) | GLUTATHIONE REDUCTASE | polymer | 450 | 48739.1 | 2 | UniProt (P06715) Pfam (PF00070) Pfam (PF02852) | Escherichia coli | |
| 2 | C, D (A, B) | FLAVIN-ADENINE DINUCLEOTIDE | non-polymer | 785.5 | 2 | Chemie (FAD) | |||
| 3 | E, F (A, B) | water | water | 18.0 | 585 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 450 (UniProt: P06715)
| PDB | External Database | Details |
|---|---|---|
| Gly 179 | Ala 179 | engineered mutation |
| Gly 183 | Ala 183 | engineered mutation |
| Glu 197 | Val 197 | engineered mutation |
| Met 198 | Arg 198 | engineered mutation |
| Phe 199 | Lys 199 | engineered mutation |
| Asp 200 | His 200 | engineered mutation |
| Pro 204 | Arg 204 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 97478.3 | |
| Non-Polymers* | Number of molecules | 2 |
| Total formula weight | 1571.1 | |
| All* | Total formula weight | 99049.4 |
