5XLX
Crystal structure of the C-terminal domain of CheR1 containing SAH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008276 | molecular_function | protein methyltransferase activity |
| A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| A | 0008983 | molecular_function | protein-glutamate O-methyltransferase activity |
| B | 0008276 | molecular_function | protein methyltransferase activity |
| B | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| B | 0008983 | molecular_function | protein-glutamate O-methyltransferase activity |
| C | 0008276 | molecular_function | protein methyltransferase activity |
| C | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| C | 0008983 | molecular_function | protein-glutamate O-methyltransferase activity |
| D | 0008276 | molecular_function | protein methyltransferase activity |
| D | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| D | 0008983 | molecular_function | protein-glutamate O-methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue SAH A 301 |
| Chain | Residue |
| A | THR74 |
| A | ASN218 |
| A | VAL219 |
| A | HOH447 |
| A | HOH463 |
| A | ARG78 |
| A | ALA109 |
| A | SER111 |
| A | GLU115 |
| A | ASP144 |
| A | ASN200 |
| A | LEU201 |
| A | ARG217 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue SAH B 301 |
| Chain | Residue |
| B | THR74 |
| B | ARG78 |
| B | ALA109 |
| B | SER111 |
| B | GLU115 |
| B | ASP144 |
| B | LEU145 |
| B | LEU199 |
| B | ASN200 |
| B | LEU201 |
| B | ARG217 |
| B | ASN218 |
| B | VAL219 |
| B | PHE223 |
| B | HOH406 |
| B | HOH465 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue SAH C 301 |
| Chain | Residue |
| C | THR74 |
| C | ARG78 |
| C | ALA109 |
| C | SER111 |
| C | GLU115 |
| C | ASP144 |
| C | LEU145 |
| C | LEU199 |
| C | ASN200 |
| C | LEU201 |
| C | ARG217 |
| C | ASN218 |
| C | VAL219 |
| C | PHE223 |
| C | HOH405 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue SAH D 301 |
| Chain | Residue |
| D | THR74 |
| D | ARG78 |
| D | ALA109 |
| D | SER111 |
| D | GLU115 |
| D | ASP144 |
| D | LEU145 |
| D | LEU199 |
| D | ASN200 |
| D | LEU201 |
| D | ARG217 |
| D | ASN218 |
| D | VAL219 |
| D | PHE223 |
| D | HOH411 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
