5DM3
Crystal Structure of Glutamine Synthetase from Chromohalobacter salexigens DSM 3043(Csal_0679, TARGET EFI-550015) with bound ADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004356 | molecular_function | glutamine synthetase activity |
| A | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| A | 1901704 | biological_process | L-glutamine biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004356 | molecular_function | glutamine synthetase activity |
| B | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| B | 1901704 | biological_process | L-glutamine biosynthetic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004356 | molecular_function | glutamine synthetase activity |
| C | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| C | 1901704 | biological_process | L-glutamine biosynthetic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004356 | molecular_function | glutamine synthetase activity |
| D | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| D | 1901704 | biological_process | L-glutamine biosynthetic process |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004356 | molecular_function | glutamine synthetase activity |
| E | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| E | 1901704 | biological_process | L-glutamine biosynthetic process |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004356 | molecular_function | glutamine synthetase activity |
| F | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| F | 1901704 | biological_process | L-glutamine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue ADP A 501 |
| Chain | Residue |
| A | ILE139 |
| A | ARG348 |
| D | LYS36 |
| D | THR51 |
| D | HIS52 |
| A | ALA141 |
| A | GLU143 |
| A | GLU201 |
| A | ILE216 |
| A | ARG217 |
| A | CYS218 |
| A | HIS264 |
| A | SER266 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue ADP B 501 |
| Chain | Residue |
| B | ILE139 |
| B | ALA141 |
| B | GLU143 |
| B | GLU201 |
| B | ILE216 |
| B | ARG217 |
| B | CYS218 |
| B | HIS264 |
| B | SER266 |
| B | ARG348 |
| C | HIS52 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue ADP C 501 |
| Chain | Residue |
| A | THR51 |
| A | HIS52 |
| C | ILE139 |
| C | ALA141 |
| C | GLU201 |
| C | ILE216 |
| C | ARG217 |
| C | CYS218 |
| C | HIS264 |
| C | SER266 |
| C | ARG348 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue ADP D 501 |
| Chain | Residue |
| D | ILE139 |
| D | ALA141 |
| D | GLU143 |
| D | GLU201 |
| D | ILE216 |
| D | ARG217 |
| D | CYS218 |
| D | HIS264 |
| D | SER266 |
| D | ARG348 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue ADP E 501 |
| Chain | Residue |
| E | ILE139 |
| E | ALA141 |
| E | GLU143 |
| E | GLU201 |
| E | ILE216 |
| E | ARG217 |
| E | CYS218 |
| E | HIS264 |
| E | SER266 |
| E | ARG348 |
| F | HIS52 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue ADP F 501 |
| Chain | Residue |
| B | HIS52 |
| F | ILE139 |
| F | ALA141 |
| F | GLU143 |
| F | GLU201 |
| F | ILE216 |
| F | CYS218 |
| F | HIS264 |
| F | SER266 |
| F | ALA346 |
| F | ARG348 |
