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 | 0009058 | biological_process | biosynthetic process |
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 | 0009058 | biological_process | biosynthetic process |
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 | 0009058 | biological_process | biosynthetic process |
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 | 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 | 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: BINDING => ECO:0000269|PubMed:21142177 |
Chain | Residue | Details |
A | TYR14 | |
B | ALA58 | |
B | GLU79 | |
B | MET117 | |
C | TYR14 | |
C | TYR22 | |
C | TYR33 | |
C | ALA58 | |
C | GLU79 | |
C | MET117 | |
D | TYR14 | |
A | TYR22 | |
D | TYR22 | |
D | TYR33 | |
D | ALA58 | |
D | GLU79 | |
D | MET117 | |
A | TYR33 | |
A | ALA58 | |
A | GLU79 | |
A | MET117 | |
B | TYR14 | |
B | TYR22 | |
B | TYR33 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP101 | |
B | ASP101 | |
C | ASP101 | |
D | ASP101 |