2D32
Crystal Structure of Michaelis Complex of gamma-Glutamylcysteine Synthetase
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B, C, D (A, B, C, D) | Glutamate--cysteine ligase | polymer | 518 | 58268.8 | 4 | UniProt (P0A6W9) Pfam (PF04262) | Escherichia coli | Gamma-glutamylcysteine synthetase, Gamma-ECS, GCS |
2 | E, F, G, H, L... (A, B, C, D) | MAGNESIUM ION | non-polymer | 24.3 | 13 | Chemie (MG) | |||
3 | AA, I, O, U (D, A, B, C) | GLUTAMIC ACID | non-polymer | 147.1 | 4 | Chemie (GLU) | |||
4 | BA, J, P, V (D, A, B, C) | CYSTEINE | non-polymer | 121.2 | 4 | Chemie (CYS) | |||
5 | CA, K, Q, W (D, A, B, C) | PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER | non-polymer | 506.2 | 4 | Chemie (ANP) | |||
6 | DA, EA, FA, GA (A, B, C, D) | water | water | 18.0 | 800 | Chemie (HOH) |
Sequence modifications
A, B, C, D: 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 | 4 |
Total formula weight | 233075.4 | |
Non-Polymers* | Number of molecules | 25 |
Total formula weight | 3413.9 | |
All* | Total formula weight | 236489.3 |