5DDW
Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with the PMP external aldimine adduct with Caerulomycin M
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 | 21 |
| Details | binding site for residue 5B6 A 601 |
| Chain | Residue |
| A | GLY120 |
| A | TYR461 |
| A | ARG486 |
| A | HOH709 |
| A | HOH739 |
| A | HOH750 |
| A | HOH752 |
| A | HOH772 |
| A | HOH788 |
| B | SER372 |
| B | THR374 |
| A | ALA121 |
| B | HOH707 |
| B | HOH737 |
| A | PHE207 |
| A | TRP223 |
| A | GLU282 |
| A | ASP315 |
| A | VAL317 |
| A | GLN318 |
| A | LYS344 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 602 |
| Chain | Residue |
| A | ARG197 |
| A | ALA229 |
| A | SER231 |
| B | ARG197 |
| B | ALA229 |
| B | LEU230 |
| B | SER231 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 603 |
| Chain | Residue |
| A | GLU27 |
| A | TYR28 |
| A | VAL29 |
| A | HOH740 |
| B | THR79 |
| B | VAL80 |
| B | ARG90 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | binding site for residue 5B6 B 601 |
| Chain | Residue |
| A | SER372 |
| A | THR374 |
| A | HOH729 |
| B | SER119 |
| B | GLY120 |
| B | ALA121 |
| B | PHE207 |
| B | TRP223 |
| B | GLU282 |
| B | ASP315 |
| B | VAL317 |
| B | GLN318 |
| B | LYS344 |
| B | TYR461 |
| B | ARG486 |
| B | HOH719 |
| B | HOH720 |
| B | HOH727 |
| B | HOH745 |
| B | HOH781 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | binding site for residue 5B6 C 601 |
| Chain | Residue |
| C | SER119 |
| C | GLY120 |
| C | ALA121 |
| C | PHE207 |
| C | HIS208 |
| C | GLU282 |
| C | ASP315 |
| C | VAL317 |
| C | GLN318 |
| C | LYS344 |
| C | TYR461 |
| C | ARG486 |
| C | HOH706 |
| C | HOH740 |
| C | HOH750 |
| C | HOH768 |
| C | HOH780 |
| C | HOH784 |
| C | HOH791 |
| D | SER372 |
| D | THR374 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 602 |
| Chain | Residue |
| C | ARG197 |
| C | ALA229 |
| C | LEU230 |
| C | SER231 |
| D | ARG197 |
| D | ALA229 |
| D | SER231 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 603 |
| Chain | Residue |
| C | THR79 |
| C | VAL80 |
| C | ARG90 |
| C | HOH783 |
| D | GLU27 |
| D | TYR28 |
| D | VAL29 |
| site_id | AC8 |
| Number of Residues | 23 |
| Details | binding site for residue 5B6 D 601 |
| Chain | Residue |
| D | HIS208 |
| D | GLU282 |
| D | ASP315 |
| D | VAL317 |
| D | GLN318 |
| D | LYS344 |
| D | TYR461 |
| D | ARG486 |
| D | HOH720 |
| D | HOH733 |
| D | HOH737 |
| D | HOH756 |
| D | HOH776 |
| D | HOH781 |
| C | SER372 |
| C | THR374 |
| C | HOH727 |
| C | HOH767 |
| D | PHE55 |
| D | SER119 |
| D | GLY120 |
| D | ALA121 |
| D | PHE207 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL D 602 |
| Chain | Residue |
| C | GLU27 |
| C | TYR28 |
| C | VAL29 |
| D | VAL80 |
| D | ARG90 |
