6FZ6
Crystal Structure of a radical SAM methyltransferase from Sphaerobacter thermophilus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0002935 | molecular_function | tRNA (adenine(37)-C2)-methyltransferase activity |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006364 | biological_process | rRNA processing |
| A | 0008173 | molecular_function | RNA methyltransferase activity |
| A | 0019843 | molecular_function | rRNA binding |
| A | 0030488 | biological_process | tRNA methylation |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 0070040 | molecular_function | rRNA (adenine(2503)-C2-)-methyltransferase activity |
| A | 0070475 | biological_process | rRNA base methylation |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0002935 | molecular_function | tRNA (adenine(37)-C2)-methyltransferase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006364 | biological_process | rRNA processing |
| B | 0008173 | molecular_function | RNA methyltransferase activity |
| B | 0019843 | molecular_function | rRNA binding |
| B | 0030488 | biological_process | tRNA methylation |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0070040 | molecular_function | rRNA (adenine(2503)-C2-)-methyltransferase activity |
| B | 0070475 | biological_process | rRNA base methylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 A 401 |
| Chain | Residue |
| A | CYS110 |
| A | VAL112 |
| A | GLY113 |
| A | CYS114 |
| A | CYS117 |
| A | GLY120 |
| A | SER194 |
| A | SAH402 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue SAH A 402 |
| Chain | Residue |
| A | CYS117 |
| A | MET157 |
| A | GLY158 |
| A | GLY160 |
| A | GLU161 |
| A | SER192 |
| A | THR193 |
| A | SER215 |
| A | HIS217 |
| A | GLU257 |
| A | VAL259 |
| A | LEU290 |
| A | ASN291 |
| A | SMC334 |
| A | GLY335 |
| A | SF4401 |
| A | HOH595 |
| A | HOH688 |
| A | PHE116 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | LEU223 |
| A | VAL264 |
| A | ASP266 |
| A | SER267 |
| A | ASN270 |
| A | HOH505 |
| A | HOH524 |
| A | HOH592 |
| A | HOH630 |
| B | TYR23 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue BR A 404 |
| Chain | Residue |
| A | ARG24 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 B 401 |
| Chain | Residue |
| B | CYS110 |
| B | VAL112 |
| B | GLY113 |
| B | CYS114 |
| B | CYS117 |
| B | GLY120 |
| B | SER194 |
| B | SAH402 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | binding site for residue SAH B 402 |
| Chain | Residue |
| B | PHE116 |
| B | CYS117 |
| B | MET157 |
| B | GLY158 |
| B | GLY160 |
| B | GLU161 |
| B | SER192 |
| B | THR193 |
| B | SER215 |
| B | HIS217 |
| B | GLU257 |
| B | VAL259 |
| B | LEU290 |
| B | ASN291 |
| B | SMC334 |
| B | GLY335 |
| B | SF4401 |
| B | HOH677 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue BR B 403 |
| Chain | Residue |
| B | ARG24 |
