4LNK
B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of GS-glutamate-AMPPCP complex
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, E... | Glutamine synthetase | polymer | 443 | 50206.9 | 6 | UniProt (P12425) Pfam (PF03951) Pfam (PF00120) In PDB | Bacillus subtilis | Glutamate--ammonia ligase |
| 2 | F, A, B, C, D... | GLUTAMIC ACID | non-polymer | 147.1 | 6 | Chemie (GLU) | |||
| 3 | F, A, B, C, D... | ADENOSINE-5'-DIPHOSPHATE | non-polymer | 427.2 | 6 | Chemie (ADP) | |||
| 4 | E, F, A, B, C... | MAGNESIUM ION | non-polymer | 24.3 | 12 | Chemie (MG) | |||
| 5 | E, A | SULFATE ION | non-polymer | 96.1 | 3 | Chemie (SO4) | |||
| 6 | water | water | 18.0 | 57 | Chemie (HOH) |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 6 |
| Total formula weight | 301241.4 | |
| Non-Polymers* | Number of molecules | 27 |
| Total formula weight | 4025.8 | |
| All* | Total formula weight | 305267.3 |
