6JC9
Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with amino donor L-Gln
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue PLP A 601 |
| Chain | Residue |
| A | SER119 |
| A | LYS344 |
| A | HOH707 |
| A | HOH780 |
| A | HOH790 |
| B | SER373 |
| B | THR374 |
| B | HOH720 |
| A | GLY120 |
| A | ALA121 |
| A | PHE207 |
| A | HIS208 |
| A | GLU282 |
| A | ASP315 |
| A | VAL317 |
| A | GLN318 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ACY B 602 |
| Chain | Residue |
| B | GLU66 |
| B | HIS70 |
| B | LYS387 |
| D | ALA69 |
| D | ASP76 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 602 |
| Chain | Residue |
| C | GLU27 |
| C | TYR28 |
| C | HOH755 |
| D | THR79 |
| D | VAL80 |
| D | ARG90 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GLN C 603 |
| Chain | Residue |
| C | SER372 |
| C | THR374 |
| C | HOH776 |
| D | PHE55 |
| D | PHE207 |
| D | GLN318 |
| D | LYS344 |
| D | PLP601 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | binding site for Di-peptide PLP B 601 and LYS B 344 |
| Chain | Residue |
| A | THR374 |
| A | HOH723 |
| B | PHE55 |
| B | SER57 |
| B | SER119 |
| B | GLY120 |
| B | ALA121 |
| B | PHE207 |
| B | HIS208 |
| B | GLU282 |
| B | ASP315 |
| B | VAL317 |
| B | GLN318 |
| B | ALA343 |
| B | ALA345 |
| B | ILE346 |
| B | GLY347 |
| B | HOH703 |
| B | HOH709 |
| B | HOH715 |
| B | HOH746 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide PLP C 601 and LYS C 344 |
| Chain | Residue |
| C | PHE55 |
| C | SER57 |
| C | SER119 |
| C | GLY120 |
| C | ALA121 |
| C | PHE207 |
| C | GLU282 |
| C | ASP315 |
| C | VAL317 |
| C | GLN318 |
| C | ALA343 |
| C | ALA345 |
| C | ILE346 |
| C | GLY347 |
| C | HOH701 |
| C | HOH724 |
| C | HOH728 |
| C | HOH775 |
| D | THR374 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | binding site for Di-peptide PLP D 601 and LYS D 344 |
| Chain | Residue |
| C | THR374 |
| C | GLN603 |
| C | HOH716 |
| D | PHE55 |
| D | SER57 |
| D | SER119 |
| D | GLY120 |
| D | ALA121 |
| D | PHE207 |
| D | HIS208 |
| D | GLU282 |
| D | ASP315 |
| D | VAL317 |
| D | GLN318 |
| D | ALA343 |
| D | ALA345 |
| D | ILE346 |
| D | GLY347 |
| D | HOH703 |
| D | HOH739 |
| D | HOH785 |
