1VA6
Crystal structure of Gamma-glutamylcysteine synthetase from Escherichia Coli B complexed with Transition-state analogue
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) | Glutamate--cysteine ligase | polymer | 518 | 58268.8 | 2 | UniProt (P0A6W9) Pfam (PF04262) | Escherichia coli | Gamma-glutamylcysteine synthetase, Gamma-ECS, GCS |
| 2 | C, D, E, F, J... (A, B) | MAGNESIUM ION | non-polymer | 24.3 | 8 | Chemie (MG) | |||
| 3 | G, N (A, B) | (2S)-2-AMINO-4-[[(2R)-2-CARBOXYBUTYL](PHOSPHONO)SULFONIMIDOYL]BUTANOIC ACID | non-polymer | 346.3 | 2 | Chemie (P2S) | |||
| 4 | H, O (A, B) | ADENOSINE-5'-DIPHOSPHATE | non-polymer | 427.2 | 2 | Chemie (ADP) | |||
| 5 | I, P (A, B) | HEXAETHYLENE GLYCOL | non-polymer | 282.3 | 2 | Chemie (P6G) | |||
| 6 | Q, R (A, B) | water | water | 18.0 | 346 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 518 (UniProt: P0A6W9)
| PDB | External Database | Details |
|---|---|---|
| Ser 106 | Cys 106 | engineered mutation |
| Ser 164 | Cys 164 | engineered mutation |
| Ser 205 | Cys 205 | engineered mutation |
| Ser 223 | Cys 223 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 116537.7 | |
| Non-Polymers* | Number of molecules | 14 |
| Total formula weight | 2306.1 | |
| All* | Total formula weight | 118843.8 |
