6VFN
Crystal structure of SpeG allosteric polyamine acetyltransferase from Bacillus thuringiensis in complex with spermine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| E | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| F | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| G | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| H | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| I | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| J | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| K | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| L | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue SPM A 201 |
| Chain | Residue |
| A | ASN22 |
| F | ASP52 |
| F | GLN53 |
| F | GLU55 |
| F | ARG56 |
| A | MET28 |
| A | GLU33 |
| A | GLU34 |
| A | TYR36 |
| A | GLU37 |
| A | GLU41 |
| F | HIS49 |
| F | ILE50 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue SPM B 201 |
| Chain | Residue |
| A | HIS49 |
| A | ILE50 |
| A | ASP52 |
| A | GLN53 |
| A | GLU55 |
| A | ARG56 |
| B | ASN22 |
| B | MET28 |
| B | GLU33 |
| B | TYR36 |
| B | GLU37 |
| B | GLU41 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue SPM C 201 |
| Chain | Residue |
| B | HIS49 |
| B | ILE50 |
| B | ASP52 |
| B | GLN53 |
| B | GLU55 |
| B | ARG56 |
| C | ASN22 |
| C | MET28 |
| C | GLU33 |
| C | GLU34 |
| C | TYR36 |
| C | GLU37 |
| C | GLU41 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue SPM D 201 |
| Chain | Residue |
| C | HIS49 |
| C | ILE50 |
| C | ASP52 |
| C | GLN53 |
| C | GLU55 |
| D | ASN22 |
| D | MET28 |
| D | GLU33 |
| D | GLU34 |
| D | TYR36 |
| D | GLU37 |
| D | GLU41 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue SPM E 201 |
| Chain | Residue |
| E | ASN22 |
| E | MET28 |
| E | GLU33 |
| E | GLU34 |
| E | TYR36 |
| E | GLU37 |
| E | GLU41 |
| H | HIS49 |
| H | ILE50 |
| H | ASP52 |
| H | GLN53 |
| H | GLU55 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue SPM E 202 |
| Chain | Residue |
| E | HIS49 |
| E | ILE50 |
| E | ASP52 |
| E | GLN53 |
| E | GLU55 |
| E | ARG56 |
| I | GLU33 |
| I | GLU34 |
| I | TYR36 |
| I | GLU37 |
| I | GLU41 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue SPM F 201 |
| Chain | Residue |
| F | ASN22 |
| F | MET28 |
| F | GLU33 |
| F | GLU34 |
| F | TYR36 |
| F | GLU37 |
| F | GLU41 |
| J | HIS49 |
| J | ILE50 |
| J | ASP52 |
| J | GLN53 |
| J | GLU55 |
| J | ARG56 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | binding site for residue SPM G 201 |
| Chain | Residue |
| G | ASN22 |
| G | MET28 |
| G | GLU33 |
| G | GLU34 |
| G | TYR36 |
| G | GLU37 |
| G | GLU41 |
| I | HIS49 |
| I | ILE50 |
| I | ASP52 |
| I | GLN53 |
| I | GLU55 |
| I | ARG56 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | binding site for residue SPM H 201 |
| Chain | Residue |
| H | ASN22 |
| H | MET28 |
| H | GLU33 |
| H | TYR36 |
| H | GLU37 |
| H | GLU41 |
| L | HIS49 |
| L | ILE50 |
| L | ASP52 |
| L | GLN53 |
| L | GLU55 |
| L | ARG56 |
| site_id | AD1 |
| Number of Residues | 12 |
| Details | binding site for residue SPM J 201 |
| Chain | Residue |
| D | HIS49 |
| D | ILE50 |
| D | ASP52 |
| D | GLN53 |
| D | GLU55 |
| D | ARG56 |
| J | ASN22 |
| J | MET28 |
| J | GLU33 |
| J | TYR36 |
| J | GLU37 |
| J | GLU41 |
| site_id | AD2 |
| Number of Residues | 13 |
| Details | binding site for residue SPM K 201 |
| Chain | Residue |
| G | HIS49 |
| G | ILE50 |
| G | ASP52 |
| G | GLN53 |
| G | GLU55 |
| G | ARG56 |
| K | ASN22 |
| K | MET28 |
| K | GLU33 |
| K | GLU34 |
| K | TYR36 |
| K | GLU37 |
| K | GLU41 |
| site_id | AD3 |
| Number of Residues | 12 |
| Details | binding site for residue SPM L 201 |
| Chain | Residue |
| K | HIS49 |
| K | ILE50 |
| K | ASP52 |
| K | GLN53 |
| K | GLU55 |
| L | ASN22 |
| L | MET28 |
| L | GLU33 |
| L | GLU34 |
| L | TYR36 |
| L | GLU37 |
| L | GLU41 |
