4OQD
Crystal structure of the tylM1 N,N-dimethyltransferase in complex with SAH and TDP-Qui3NMe2
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 |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0032259 | biological_process | methylation |
| C | 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 | 24 |
| Details | BINDING SITE FOR RESIDUE SAH A 300 |
| Chain | Residue |
| A | TYR14 |
| A | MET84 |
| A | GLY100 |
| A | ASP101 |
| A | MET102 |
| A | MET117 |
| A | PHE118 |
| A | SER120 |
| A | HIS123 |
| A | QDM301 |
| A | HOH401 |
| A | TYR22 |
| A | HOH417 |
| A | HOH418 |
| A | HOH425 |
| A | HOH431 |
| A | HOH508 |
| 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 QDM A 301 |
| Chain | Residue |
| A | TYR14 |
| A | HIS26 |
| A | LYS29 |
| A | PHE118 |
| A | TRP152 |
| A | TRP153 |
| A | ASN157 |
| A | PHE158 |
| A | THR159 |
| A | TYR162 |
| A | ARG177 |
| A | SER179 |
| A | SER181 |
| A | ILE190 |
| A | ARG241 |
| A | SAH300 |
| A | HOH403 |
| A | HOH404 |
| A | HOH472 |
| site_id | AC3 |
| Number of Residues | 23 |
| 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 | GLY100 |
| B | ASP101 |
| B | MET102 |
| B | MET117 |
| B | PHE118 |
| B | SER120 |
| B | QDM301 |
| B | HOH410 |
| B | HOH416 |
| B | HOH432 |
| B | HOH433 |
| B | HOH477 |
| B | HOH518 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE QDM B 301 |
| Chain | Residue |
| B | TYR14 |
| B | HIS26 |
| B | LYS29 |
| B | PHE118 |
| B | TRP152 |
| B | TRP153 |
| B | ASN157 |
| B | PHE158 |
| B | THR159 |
| B | TYR162 |
| B | ARG177 |
| B | SER179 |
| B | SER181 |
| B | ILE190 |
| B | HIS210 |
| B | ARG241 |
| B | SAH300 |
| B | HOH404 |
| B | HOH462 |
| B | HOH479 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SAH C 300 |
| Chain | Residue |
| C | ARG103 |
| C | MET117 |
| C | PHE118 |
| C | SER120 |
| C | QDM301 |
| C | HOH417 |
| C | HOH420 |
| C | HOH430 |
| C | HOH494 |
| C | TYR14 |
| C | TYR22 |
| C | TYR33 |
| C | ALA58 |
| C | GLY60 |
| C | HIS64 |
| C | GLU79 |
| C | LEU80 |
| C | SER81 |
| C | MET84 |
| C | GLY100 |
| C | ASP101 |
| C | MET102 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE QDM C 301 |
| Chain | Residue |
| C | TYR14 |
| C | HIS26 |
| C | LYS29 |
| C | PHE118 |
| C | SER119 |
| C | TRP152 |
| C | TRP153 |
| C | ASN157 |
| C | PHE158 |
| C | THR159 |
| C | TYR162 |
| C | ARG177 |
| C | SER179 |
| C | SER181 |
| C | ILE190 |
| C | HIS210 |
| C | ARG241 |
| C | SAH300 |
| C | HOH404 |
| C | HOH501 |
| C | HOH555 |
| site_id | AC7 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE SAH D 300 |
| Chain | Residue |
| D | TYR14 |
| D | TYR22 |
| D | TYR33 |
| D | ALA58 |
| D | CYS59 |
| D | GLY60 |
| D | HIS64 |
| D | GLU79 |
| D | LEU80 |
| D | SER81 |
| D | MET84 |
| D | GLY100 |
| D | ASP101 |
| D | MET102 |
| D | MET117 |
| D | PHE118 |
| D | SER120 |
| D | HIS123 |
| D | QDM301 |
| D | HOH408 |
| D | HOH409 |
| D | HOH410 |
| D | HOH471 |
| D | HOH532 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE QDM D 301 |
| Chain | Residue |
| D | TYR14 |
| D | HIS26 |
| D | LYS29 |
| D | PHE118 |
| D | TRP152 |
| D | TRP153 |
| D | ASN157 |
| D | PHE158 |
| D | THR159 |
| D | TYR162 |
| D | ARG177 |
| D | SER179 |
| D | SER181 |
| D | ILE190 |
| D | HIS210 |
| D | ARG241 |
| D | SAH300 |
| D | HOH404 |
| D | HOH459 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21142177","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
