3PFH
X-Ray crystal structure the N,N-dimethyltransferase TylM1 from Streptomyces fradiae in complex with SAH and dTDP-Quip3N
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0032259 | biological_process | methylation |
| A | 0042803 | molecular_function | protein homodimerization activity |
| D | 0008168 | molecular_function | methyltransferase activity |
| D | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 0032259 | biological_process | methylation |
| D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE SAH A 264 |
| Chain | Residue |
| A | TYR14 |
| A | GLY100 |
| A | ASP101 |
| A | MET102 |
| A | MET117 |
| A | PHE118 |
| A | SER120 |
| A | HIS123 |
| A | HOH274 |
| A | HOH276 |
| A | HOH294 |
| A | TYR22 |
| A | T3Q301 |
| A | HOH307 |
| A | HOH448 |
| A | HOH450 |
| A | TYR33 |
| A | ALA58 |
| A | GLY60 |
| A | HIS64 |
| A | GLU79 |
| A | LEU80 |
| A | MET84 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE T3Q A 301 |
| Chain | Residue |
| A | TYR14 |
| A | HIS26 |
| A | LYS29 |
| A | PHE118 |
| A | TRP152 |
| A | TRP153 |
| A | PHE158 |
| A | THR159 |
| A | TYR162 |
| A | ALA164 |
| A | ARG177 |
| A | SER179 |
| A | SER181 |
| A | ILE190 |
| A | HIS210 |
| A | ARG241 |
| A | SAH264 |
| A | HOH290 |
| A | HOH302 |
| A | HOH386 |
| A | HOH398 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 265 |
| Chain | Residue |
| A | GLY126 |
| A | GLU186 |
| A | PHE215 |
| A | GLN219 |
| A | HOH383 |
| A | HOH519 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SAH D 264 |
| Chain | Residue |
| D | TYR14 |
| D | TYR22 |
| D | TYR33 |
| D | ALA58 |
| D | GLY60 |
| D | HIS64 |
| D | GLU79 |
| D | LEU80 |
| D | MET84 |
| D | ASP101 |
| D | MET102 |
| D | MET117 |
| D | PHE118 |
| D | SER120 |
| D | HIS123 |
| D | HOH268 |
| D | HOH278 |
| D | HOH282 |
| D | T3Q301 |
| D | HOH334 |
| D | HOH347 |
| D | HOH418 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE T3Q D 301 |
| Chain | Residue |
| D | TYR14 |
| D | HIS26 |
| D | LYS29 |
| D | PHE118 |
| D | TRP152 |
| D | TRP153 |
| D | PHE158 |
| D | THR159 |
| D | TYR162 |
| D | ALA164 |
| D | ARG177 |
| D | SER179 |
| D | SER181 |
| D | HIS210 |
| D | ARG241 |
| D | SAH264 |
| D | HOH266 |
| D | HOH270 |
| D | HOH310 |
| D | HOH327 |
| D | HOH403 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21142177","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
