4LNI
B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of the transition state 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 | 12 | UniProt (P12425) Pfam (PF03951) Pfam (PF00120) In PDB | Bacillus subtilis | Glutamate--ammonia ligase |
| 2 | I, D, J, E, K... | L-METHIONINE-S-SULFOXIMINE PHOSPHATE | non-polymer | 260.2 | 12 | Chemie (P3S) | |||
| 3 | I, D, J, E, K... | ADENOSINE-5'-DIPHOSPHATE | non-polymer | 427.2 | 12 | Chemie (ADP) | |||
| 4 | C, I, D, J, E... | MAGNESIUM ION | non-polymer | 24.3 | 36 | Chemie (MG) | |||
| 5 | water | water | 18.0 | 2167 | Chemie (HOH) |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 12 |
| Total formula weight | 602482.9 | |
| Non-Polymers* | Number of molecules | 60 |
| Total formula weight | 9123.9 | |
| All* | Total formula weight | 611606.7 |
