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 | 0009058 | biological_process | biosynthetic process |
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 | 0009058 | biological_process | biosynthetic process |
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: BINDING => ECO:0000269|PubMed:21142177 |
Chain | Residue | Details |
A | TYR14 | |
D | ALA58 | |
D | GLU79 | |
D | MET117 | |
A | TYR22 | |
A | TYR33 | |
A | ALA58 | |
A | GLU79 | |
A | MET117 | |
D | TYR14 | |
D | TYR22 | |
D | TYR33 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP101 | |
D | ASP101 |