3SSM
MycE Methyltransferase from the Mycinamycin Biosynthetic Pathway in Complex with Mg and SAH, Crystal form 1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008171 | molecular_function | O-methyltransferase activity |
A | 0017000 | biological_process | antibiotic biosynthetic process |
A | 0032259 | biological_process | methylation |
A | 0046872 | molecular_function | metal ion binding |
A | 0051289 | biological_process | protein homotetramerization |
A | 0102302 | molecular_function | mycinamicin VI 2''-O-methyltransferase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0008171 | molecular_function | O-methyltransferase activity |
B | 0017000 | biological_process | antibiotic biosynthetic process |
B | 0032259 | biological_process | methylation |
B | 0046872 | molecular_function | metal ion binding |
B | 0051289 | biological_process | protein homotetramerization |
B | 0102302 | molecular_function | mycinamicin VI 2''-O-methyltransferase activity |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0008168 | molecular_function | methyltransferase activity |
C | 0008171 | molecular_function | O-methyltransferase activity |
C | 0017000 | biological_process | antibiotic biosynthetic process |
C | 0032259 | biological_process | methylation |
C | 0046872 | molecular_function | metal ion binding |
C | 0051289 | biological_process | protein homotetramerization |
C | 0102302 | molecular_function | mycinamicin VI 2''-O-methyltransferase activity |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0008168 | molecular_function | methyltransferase activity |
D | 0008171 | molecular_function | O-methyltransferase activity |
D | 0017000 | biological_process | antibiotic biosynthetic process |
D | 0032259 | biological_process | methylation |
D | 0046872 | molecular_function | metal ion binding |
D | 0051289 | biological_process | protein homotetramerization |
D | 0102302 | molecular_function | mycinamicin VI 2''-O-methyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 501 |
Chain | Residue |
A | ASP275 |
A | GLU303 |
A | ASP304 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE SAH A 601 |
Chain | Residue |
A | TYR208 |
A | SER217 |
A | ASP234 |
A | ILE235 |
A | GLY251 |
A | ASP252 |
A | GLN253 |
A | ASP275 |
A | GLY276 |
A | SER277 |
A | HOH703 |
A | HOH741 |
D | PHE387 |
A | THR173 |
A | PRO174 |
A | LYS175 |
A | GLU202 |
A | GLY204 |
A | GLY206 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG C 501 |
Chain | Residue |
C | ASP275 |
C | GLU303 |
C | ASP304 |
C | HOH713 |
site_id | AC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE SAH C 601 |
Chain | Residue |
B | PHE387 |
C | THR173 |
C | LYS175 |
C | GLU202 |
C | GLY204 |
C | VAL205 |
C | GLY206 |
C | TYR208 |
C | SER217 |
C | ASP234 |
C | ILE235 |
C | GLY251 |
C | ASP252 |
C | GLN253 |
C | ASP275 |
C | GLY276 |
C | SER277 |
C | HIS282 |
C | HOH498 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG D 501 |
Chain | Residue |
D | ASP275 |
D | GLU303 |
D | ASP304 |
D | HOH704 |
site_id | AC6 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE SAH D 601 |
Chain | Residue |
A | PHE387 |
D | THR173 |
D | LYS175 |
D | GLU202 |
D | GLY204 |
D | GLY206 |
D | TYR208 |
D | SER217 |
D | ASP234 |
D | ILE235 |
D | GLY251 |
D | ASP252 |
D | GLN253 |
D | ASP275 |
D | GLY276 |
D | SER277 |
D | HIS282 |
D | HOH533 |
D | HOH704 |
D | HOH901 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:21884704 |
Chain | Residue | Details |
A | HIS278 | |
B | HIS278 | |
C | HIS278 | |
D | HIS278 |
site_id | SWS_FT_FI2 |
Number of Residues | 32 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21884704 |
Chain | Residue | Details |
A | THR173 | |
B | GLU202 | |
B | SER217 | |
B | ASP234 | |
B | ASP252 | |
B | ASP275 | |
B | GLU303 | |
B | ASP304 | |
C | THR173 | |
C | GLU202 | |
C | SER217 | |
A | GLU202 | |
C | ASP234 | |
C | ASP252 | |
C | ASP275 | |
C | GLU303 | |
C | ASP304 | |
D | THR173 | |
D | GLU202 | |
D | SER217 | |
D | ASP234 | |
D | ASP252 | |
A | SER217 | |
D | ASP275 | |
D | GLU303 | |
D | ASP304 | |
A | ASP234 | |
A | ASP252 | |
A | ASP275 | |
A | GLU303 | |
A | ASP304 | |
B | THR173 |