3SMA
A new N-acetyltransferase fold in the structure and mechanism of the phosphonate biosynthetic enzyme FrbF
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0046353 | molecular_function | aminoglycoside 3-N-acetyltransferase activity |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0046353 | molecular_function | aminoglycoside 3-N-acetyltransferase activity |
| B | 0046677 | biological_process | response to antibiotic |
| C | 0016746 | molecular_function | acyltransferase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0046353 | molecular_function | aminoglycoside 3-N-acetyltransferase activity |
| C | 0046677 | biological_process | response to antibiotic |
| D | 0016746 | molecular_function | acyltransferase activity |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 0046353 | molecular_function | aminoglycoside 3-N-acetyltransferase activity |
| D | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ACO A 300 |
| Chain | Residue |
| A | ARG19 |
| A | PRO78 |
| A | PHE80 |
| A | GLY119 |
| A | MET120 |
| A | GLY121 |
| A | ALA122 |
| A | CYS184 |
| A | GLU187 |
| A | SER188 |
| A | THR190 |
| A | HIS45 |
| A | HIS193 |
| A | GLU231 |
| A | HOH299 |
| A | HOH318 |
| A | ALA46 |
| A | SER47 |
| A | LEU48 |
| A | SER49 |
| A | GLY52 |
| A | VAL54 |
| A | GLY57 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ACO B 300 |
| Chain | Residue |
| B | HIS45 |
| B | ALA46 |
| B | SER47 |
| B | LEU48 |
| B | SER49 |
| B | GLY52 |
| B | VAL54 |
| B | GLY57 |
| B | PRO78 |
| B | PHE80 |
| B | MET120 |
| B | GLY121 |
| B | ALA122 |
| B | CYS184 |
| B | GLU187 |
| B | SER188 |
| B | THR190 |
| B | HIS193 |
| B | GLU231 |
| B | HOH320 |
| B | HOH342 |
| B | HOH358 |
| B | HOH387 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ACO C 300 |
| Chain | Residue |
| C | HIS45 |
| C | ALA46 |
| C | SER47 |
| C | LEU48 |
| C | SER49 |
| C | GLY52 |
| C | VAL54 |
| C | GLY57 |
| C | LYS71 |
| C | PRO78 |
| C | GLY121 |
| C | ALA122 |
| C | CYS184 |
| C | GLU187 |
| C | SER188 |
| C | THR190 |
| C | HIS193 |
| C | HOH298 |
| C | HOH328 |
| C | HOH362 |
| C | HOH393 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ACO D 300 |
| Chain | Residue |
| D | ARG19 |
| D | HIS45 |
| D | ALA46 |
| D | SER47 |
| D | LEU48 |
| D | SER49 |
| D | GLY52 |
| D | VAL54 |
| D | GLY57 |
| D | PRO78 |
| D | MET120 |
| D | GLY121 |
| D | ALA122 |
| D | CYS184 |
| D | GLU187 |
| D | SER188 |
| D | THR190 |
| D | HIS193 |
| D | GLU231 |
| D | HOH290 |
| D | HOH304 |
| D | HOH423 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21865168, ECO:0007744|PDB:3SMA |
| Chain | Residue | Details |
| A | HIS45 | |
| B | HIS45 | |
| B | ALA46 | |
| B | SER47 | |
| B | LEU48 | |
| B | SER49 | |
| B | VAL54 | |
| B | ALA122 | |
| B | SER188 | |
| B | THR190 | |
| C | HIS45 | |
| A | ALA46 | |
| C | ALA46 | |
| C | SER47 | |
| C | LEU48 | |
| C | SER49 | |
| C | VAL54 | |
| C | ALA122 | |
| C | SER188 | |
| C | THR190 | |
| D | HIS45 | |
| D | ALA46 | |
| A | SER47 | |
| D | SER47 | |
| D | LEU48 | |
| D | SER49 | |
| D | VAL54 | |
| D | ALA122 | |
| D | SER188 | |
| D | THR190 | |
| A | LEU48 | |
| A | SER49 | |
| A | VAL54 | |
| A | ALA122 | |
| A | SER188 | |
| A | THR190 |
