6ERD
Crystal structure of a putative acetyltransferase from Bacillus cereus species.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008080 | molecular_function | N-acetyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008080 | molecular_function | N-acetyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0008080 | molecular_function | N-acetyltransferase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016746 | molecular_function | acyltransferase activity |
| C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008080 | molecular_function | N-acetyltransferase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016746 | molecular_function | acyltransferase activity |
| D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 301 |
| Chain | Residue |
| A | ILE58 |
| A | HOH433 |
| D | ILE88 |
| D | THR93 |
| D | LEU94 |
| D | ALA95 |
| D | HOH404 |
| D | HOH425 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | TRP70 |
| A | GLY163 |
| A | TYR165 |
| A | HOH401 |
| A | HOH405 |
| A | HOH412 |
| A | HOH423 |
| A | GLN69 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | GLU65 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 304 |
| Chain | Residue |
| A | ASP80 |
| A | GLU81 |
| D | GLU47 |
| D | SER48 |
| D | HOH489 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue GOL B 301 |
| Chain | Residue |
| B | GLN69 |
| B | TRP70 |
| B | GLY72 |
| B | GLY163 |
| B | TYR165 |
| B | CL305 |
| B | HOH405 |
| B | HOH412 |
| B | HOH415 |
| B | HOH483 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 302 |
| Chain | Residue |
| B | ILE88 |
| B | THR93 |
| B | LEU94 |
| B | ALA95 |
| B | HOH409 |
| B | HOH414 |
| B | HOH436 |
| C | ILE58 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 303 |
| Chain | Residue |
| B | ASN92 |
| B | GLN114 |
| B | ILE115 |
| B | HOH402 |
| B | HOH459 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 304 |
| Chain | Residue |
| B | SER48 |
| C | LYS55 |
| C | ASP80 |
| C | GLU81 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 305 |
| Chain | Residue |
| B | ARG123 |
| B | GOL301 |
| B | HOH405 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue GOL C 301 |
| Chain | Residue |
| C | GLN69 |
| C | TRP70 |
| C | GLY72 |
| C | GLY163 |
| C | TYR165 |
| C | HOH414 |
| C | HOH426 |
| C | HOH457 |
| C | HOH465 |
| C | HOH505 |
| site_id | AD2 |
| Number of Residues | 11 |
| Details | binding site for residue GOL D 301 |
| Chain | Residue |
| D | GLN69 |
| D | TRP70 |
| D | GLY72 |
| D | GLY125 |
| D | LYS126 |
| D | GLY163 |
| D | TYR165 |
| D | HOH410 |
| D | HOH441 |
| D | HOH458 |
| D | HOH470 |
