4OQE
Crystal structure of the tylM1 N,N-dimethyltransferase in complex with SAH and TDP-Fuc3NMe
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 |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0032259 | biological_process | methylation |
| B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SAH A 300 |
| Chain | Residue |
| A | TYR14 |
| A | ASP101 |
| A | MET102 |
| A | MET117 |
| A | PHE118 |
| A | SER120 |
| A | MMF301 |
| A | HOH409 |
| A | HOH411 |
| A | HOH428 |
| A | TYR22 |
| A | TYR33 |
| A | ALA58 |
| A | GLY60 |
| A | HIS64 |
| A | GLU79 |
| A | LEU80 |
| A | SER81 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE MMF A 301 |
| Chain | Residue |
| A | TYR14 |
| A | LYS29 |
| A | PHE118 |
| A | TRP152 |
| A | TRP153 |
| A | ASN157 |
| A | PHE158 |
| A | THR159 |
| A | TYR162 |
| A | ALA164 |
| A | ARG177 |
| A | SER179 |
| A | SER181 |
| A | ILE190 |
| A | HIS210 |
| A | ILE212 |
| A | ARG241 |
| A | SAH300 |
| A | HOH479 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SAH B 300 |
| Chain | Residue |
| B | TYR14 |
| B | TYR22 |
| B | TYR33 |
| B | ALA58 |
| B | CYS59 |
| B | GLY60 |
| B | HIS64 |
| B | GLU79 |
| B | LEU80 |
| B | SER81 |
| B | MET84 |
| B | ASP101 |
| B | MET102 |
| B | MET117 |
| B | PHE118 |
| B | SER120 |
| B | MMF301 |
| B | HOH427 |
| B | HOH465 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE MMF B 301 |
| Chain | Residue |
| B | TYR14 |
| B | LYS29 |
| B | PHE118 |
| B | HIS123 |
| B | TRP152 |
| B | TRP153 |
| B | ASN157 |
| B | PHE158 |
| B | THR159 |
| B | TYR162 |
| B | ALA164 |
| B | ARG177 |
| B | SER179 |
| B | SER181 |
| B | HIS210 |
| B | ARG241 |
| B | SAH300 |
| B | HOH444 |
| B | HOH455 |
| B | HOH459 |
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 |
