6JC8
Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with amino donor L-Glu
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 | 20 |
| Details | binding site for residue PL6 A 601 |
| Chain | Residue |
| A | PHE55 |
| A | VAL317 |
| A | GLN318 |
| A | LYS344 |
| A | HOH702 |
| A | HOH727 |
| A | HOH779 |
| A | HOH814 |
| B | SER372 |
| B | SER373 |
| B | THR374 |
| A | SER119 |
| B | HOH722 |
| A | GLY120 |
| A | ALA121 |
| A | ASN124 |
| A | PHE207 |
| A | HIS208 |
| A | GLU282 |
| A | ASP315 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 602 |
| Chain | Residue |
| A | ARG197 |
| A | ALA229 |
| A | SER231 |
| B | ARG197 |
| B | SER231 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | binding site for residue PL6 B 601 |
| Chain | Residue |
| A | SER372 |
| A | SER373 |
| A | THR374 |
| B | PHE55 |
| B | SER119 |
| B | GLY120 |
| B | ALA121 |
| B | PHE207 |
| B | HIS208 |
| B | GLU282 |
| B | ASP315 |
| B | VAL317 |
| B | GLN318 |
| B | LYS344 |
| B | HOH728 |
| B | HOH738 |
| B | HOH758 |
| B | HOH765 |
| B | HOH821 |
| B | HOH835 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | binding site for residue PL6 C 601 |
| Chain | Residue |
| C | PHE55 |
| C | SER119 |
| C | GLY120 |
| C | ALA121 |
| C | PHE207 |
| C | HIS208 |
| C | GLU282 |
| C | ASP315 |
| C | VAL317 |
| C | GLN318 |
| C | LYS344 |
| C | HOH701 |
| C | HOH711 |
| C | HOH777 |
| C | HOH786 |
| C | HOH797 |
| C | HOH816 |
| D | SER372 |
| D | SER373 |
| D | THR374 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 602 |
| Chain | Residue |
| C | ALA229 |
| C | LEU230 |
| C | SER231 |
| D | ARG197 |
| D | ALA229 |
| D | SER231 |
| D | SER232 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for residue PL6 D 601 |
| Chain | Residue |
| C | SER372 |
| C | THR374 |
| C | HOH732 |
| D | PHE55 |
| D | SER119 |
| D | GLY120 |
| D | ALA121 |
| D | PHE207 |
| D | HIS208 |
| D | GLU282 |
| D | ASP315 |
| D | VAL317 |
| D | GLN318 |
| D | LYS344 |
| D | HOH714 |
| D | HOH762 |
| D | HOH779 |
| D | HOH800 |
| D | HOH815 |
