3SSO
MycE Methyltransferase from the Mycinamycin Biosynthetic Pathway in Complex with Mg and SAH, Crystal form 2
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 |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0008168 | molecular_function | methyltransferase activity |
| E | 0008171 | molecular_function | O-methyltransferase activity |
| E | 0017000 | biological_process | antibiotic biosynthetic process |
| E | 0032259 | biological_process | methylation |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051289 | biological_process | protein homotetramerization |
| E | 0102302 | molecular_function | mycinamicin VI 2''-O-methyltransferase activity |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0008168 | molecular_function | methyltransferase activity |
| F | 0008171 | molecular_function | O-methyltransferase activity |
| F | 0017000 | biological_process | antibiotic biosynthetic process |
| F | 0032259 | biological_process | methylation |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051289 | biological_process | protein homotetramerization |
| F | 0102302 | molecular_function | mycinamicin VI 2''-O-methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | ASP275 |
| A | GLU303 |
| A | ASP304 |
| A | HOH2050 |
| A | HOH2051 |
| A | HOH2240 |
| A | HOH2360 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SAH A 601 |
| Chain | Residue |
| A | GLU202 |
| A | GLY204 |
| A | VAL205 |
| A | GLY206 |
| A | TYR208 |
| A | SER217 |
| A | ASP234 |
| A | ILE235 |
| A | GLY251 |
| A | ASP252 |
| A | GLN253 |
| A | ASP275 |
| A | GLY276 |
| A | SER277 |
| A | HIS282 |
| A | HOH1282 |
| A | HOH2033 |
| A | HOH2050 |
| A | HOH2052 |
| D | PHE387 |
| A | THR173 |
| A | LYS175 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 501 |
| Chain | Residue |
| B | ASP275 |
| B | GLU303 |
| B | ASP304 |
| B | HOH1276 |
| B | HOH1978 |
| B | HOH2806 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SAH B 601 |
| Chain | Residue |
| B | THR173 |
| B | LYS175 |
| B | GLU202 |
| B | GLY204 |
| B | VAL205 |
| B | GLY206 |
| B | TYR208 |
| B | SER217 |
| B | ASP234 |
| B | ILE235 |
| B | GLY251 |
| B | ASP252 |
| B | GLN253 |
| B | ASP275 |
| B | GLY276 |
| B | SER277 |
| B | HIS282 |
| B | HOH1900 |
| B | HOH1978 |
| B | HOH2073 |
| B | HOH2075 |
| C | PHE387 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG C 501 |
| Chain | Residue |
| C | ASP275 |
| C | GLU303 |
| C | ASP304 |
| C | HOH2063 |
| C | HOH2064 |
| C | HOH2065 |
| C | HOH2275 |
| site_id | AC6 |
| Number of Residues | 21 |
| 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 | HOH813 |
| C | HOH1872 |
| C | HOH1928 |
| C | HOH2064 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 501 |
| Chain | Residue |
| D | ASP275 |
| D | GLU303 |
| D | ASP304 |
| D | HOH1356 |
| D | HOH1998 |
| D | HOH2807 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE SAH D 601 |
| Chain | Residue |
| D | ASP234 |
| D | ILE235 |
| D | GLY251 |
| D | ASP252 |
| D | GLN253 |
| D | ASP275 |
| D | GLY276 |
| D | SER277 |
| D | HIS282 |
| D | HOH1886 |
| D | HOH1998 |
| D | HOH2067 |
| D | HOH2069 |
| A | PHE387 |
| D | THR173 |
| D | LYS175 |
| D | GLU202 |
| D | GLY204 |
| D | GLY206 |
| D | TYR208 |
| D | SER217 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG E 501 |
| Chain | Residue |
| E | ASP275 |
| E | GLU303 |
| E | ASP304 |
| E | HOH1354 |
| E | HOH1977 |
| E | HOH2397 |
| site_id | BC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE SAH E 601 |
| Chain | Residue |
| E | THR173 |
| E | LYS175 |
| E | GLU202 |
| E | GLY204 |
| E | VAL205 |
| E | GLY206 |
| E | TYR208 |
| E | SER217 |
| E | ASP234 |
| E | ILE235 |
| E | GLY251 |
| E | ASP252 |
| E | GLN253 |
| E | ASP275 |
| E | GLY276 |
| E | SER277 |
| E | HOH1736 |
| E | HOH1977 |
| E | HOH2070 |
| E | HOH2071 |
| F | PHE387 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 501 |
| Chain | Residue |
| F | ASP275 |
| F | GLU303 |
| F | ASP304 |
| F | HOH2059 |
| F | HOH2060 |
| F | HOH2061 |
| site_id | BC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE SAH F 601 |
| Chain | Residue |
| E | PHE387 |
| F | THR173 |
| F | LYS175 |
| F | GLU202 |
| F | GLY204 |
| F | VAL205 |
| F | GLY206 |
| F | TYR208 |
| F | SER217 |
| F | ASP234 |
| F | ILE235 |
| F | GLY251 |
| F | ASP252 |
| F | GLN253 |
| F | ASP275 |
| F | GLY276 |
| F | SER277 |
| F | HOH1046 |
| F | HOH2057 |
| F | HOH2058 |
| F | HOH2060 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:21884704 |
| Chain | Residue | Details |
| A | HIS278 | |
| B | HIS278 | |
| C | HIS278 | |
| D | HIS278 | |
| E | HIS278 | |
| F | HIS278 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 48 |
| 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 | |
| E | THR173 | |
| E | GLU202 | |
| E | SER217 | |
| E | ASP234 | |
| E | ASP252 | |
| E | ASP275 | |
| E | GLU303 | |
| A | ASP234 | |
| E | ASP304 | |
| F | THR173 | |
| F | GLU202 | |
| F | SER217 | |
| F | ASP234 | |
| F | ASP252 | |
| F | ASP275 | |
| F | GLU303 | |
| F | ASP304 | |
| A | ASP252 | |
| A | ASP275 | |
| A | GLU303 | |
| A | ASP304 | |
| B | THR173 |
