5DDU
Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with PMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0008483 | molecular_function | transaminase 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 | 13 |
| Details | binding site for residue PMP A 601 |
| Chain | Residue |
| A | SER119 |
| A | LYS344 |
| A | HOH717 |
| A | HOH738 |
| B | THR374 |
| 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 GOL A 602 |
| Chain | Residue |
| A | ALA229 |
| A | LEU230 |
| A | SER231 |
| B | ARG197 |
| B | SER231 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 603 |
| Chain | Residue |
| A | TRP18 |
| A | PHE458 |
| B | VAL369 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue PGE A 604 |
| Chain | Residue |
| A | VAL26 |
| A | GLU27 |
| A | VAL29 |
| A | LEU39 |
| B | ARG87 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue PMP B 601 |
| Chain | Residue |
| A | THR374 |
| B | SER119 |
| B | GLY120 |
| B | ALA121 |
| B | PHE207 |
| B | HIS208 |
| B | GLU282 |
| B | ASP315 |
| B | VAL317 |
| B | GLN318 |
| B | LYS344 |
| B | HOH712 |
| B | HOH755 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 602 |
| Chain | Residue |
| B | GLU296 |
| B | GLU299 |
| C | GLU296 |
| C | GLU299 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 603 |
| Chain | Residue |
| B | HIS64 |
| B | TYR492 |
| B | HOH707 |
| C | PRO65 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 604 |
| Chain | Residue |
| B | GLU66 |
| B | HIS70 |
| B | LYS387 |
| C | ALA69 |
| C | ALA73 |
| C | ASP76 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | binding site for residue PMP 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 | HOH755 |
| D | THR374 |
| D | HOH727 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 602 |
| Chain | Residue |
| C | ARG197 |
| C | THR228 |
| C | ALA229 |
| C | SER231 |
| D | ARG197 |
| D | LEU230 |
| D | SER231 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue GOL C 603 |
| Chain | Residue |
| C | HIS64 |
| C | TYR492 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 604 |
| Chain | Residue |
| C | GLU27 |
| C | TYR28 |
| C | VAL29 |
| D | VAL80 |
| D | PRO89 |
| D | ARG90 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue GOL C 605 |
| Chain | Residue |
| C | TRP18 |
| C | PHE458 |
| site_id | AD5 |
| Number of Residues | 13 |
| Details | binding site for residue PMP D 601 |
| Chain | Residue |
| C | THR374 |
| D | SER119 |
| D | GLY120 |
| D | ALA121 |
| D | PHE207 |
| D | HIS208 |
| D | GLY209 |
| D | GLU282 |
| D | ASP315 |
| D | VAL317 |
| D | GLN318 |
| D | LYS344 |
| D | HOH710 |
