3PX2
Structure of TylM1 from Streptomyces fradiae H123N mutant 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 | 22 |
| Details | BINDING SITE FOR RESIDUE SAH A 263 |
| Chain | Residue |
| A | TYR14 |
| A | MET84 |
| A | ASP101 |
| A | MET102 |
| A | MET117 |
| A | PHE118 |
| A | SER120 |
| A | ASN123 |
| A | HOH264 |
| A | HOH286 |
| A | HOH287 |
| A | TYR22 |
| A | T3Q301 |
| A | HOH324 |
| A | HOH444 |
| A | TYR33 |
| A | ALA58 |
| A | GLY60 |
| A | HIS64 |
| A | GLU79 |
| A | LEU80 |
| A | SER81 |
| site_id | AC2 |
| Number of Residues | 20 |
| 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 | ARG241 |
| A | SAH263 |
| A | HOH274 |
| A | HOH294 |
| A | HOH307 |
| A | HOH319 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE SAH D 263 |
| Chain | Residue |
| D | TYR14 |
| D | TYR22 |
| D | TYR33 |
| D | ALA58 |
| D | GLY60 |
| D | HIS64 |
| D | GLU79 |
| D | LEU80 |
| D | ASP101 |
| D | MET102 |
| D | ARG103 |
| D | MET117 |
| D | PHE118 |
| D | SER120 |
| D | ASN123 |
| D | HOH278 |
| D | HOH284 |
| D | HOH297 |
| D | T3Q301 |
| D | HOH384 |
| site_id | AC4 |
| 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 | ILE190 |
| D | HIS210 |
| D | ARG241 |
| D | SAH263 |
| D | HOH277 |
| D | HOH282 |
| D | HOH353 |
| D | HOH383 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 264 |
| Chain | Residue |
| D | TRP153 |
| D | ASN157 |
| D | PRO235 |
| D | GLY236 |
| D | GLY240 |
| D | ARG241 |
| D | GLY242 |
| D | HOH296 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 265 |
| Chain | Residue |
| D | GLU156 |
| D | PHE158 |
| D | THR159 |
| D | HOH274 |
| D | HOH529 |
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 |
