6ERD
Crystal structure of a putative acetyltransferase from Bacillus cereus species.
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 |
A | 0047663 | molecular_function | aminoglycoside 6'-N-acetyltransferase 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 |
B | 0047663 | molecular_function | aminoglycoside 6'-N-acetyltransferase 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 |
C | 0047663 | molecular_function | aminoglycoside 6'-N-acetyltransferase 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 |
D | 0047663 | molecular_function | aminoglycoside 6'-N-acetyltransferase activity |
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 |