Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006935 | biological_process | chemotaxis |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| A | 0008983 | molecular_function | protein-glutamate O-methyltransferase activity |
| A | 0032259 | biological_process | methylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO A 300 |
| Chain | Residue |
| A | HIS114 |
| A | HIS192 |
| A | HOH388 |
| T | HOH26 |
| T | HOH27 |
| T | HOH92 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SAH A 287 |
| Chain | Residue |
| A | THR90 |
| A | THR91 |
| A | ASN92 |
| A | LEU93 |
| A | THR94 |
| A | ARG98 |
| A | ALA123 |
| A | SER125 |
| A | GLU129 |
| A | ASP154 |
| A | ILE155 |
| A | ASP156 |
| A | VAL211 |
| A | ASN212 |
| A | LEU213 |
| A | ARG230 |
| A | ASN231 |
| A | VAL232 |
| A | PHE236 |
| A | HOH327 |
| A | HOH378 |
| A | ALA38 |
| site_id | COB |
| Number of Residues | 2 |
| Details | CO BINDING SITE IS FORMED BY HIS 192 AND HIS 114 OF THE SYMMETRY RELATED MOLECULE. THIS IS AN ARTIFACT OF THE CRYSTALLIZATION AND HAS NO PHYSIOLOGICAL SIGNIFICANCE. |
| Chain | Residue |
| A | HIS192 |
| A | HIS114 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN92 | |
| A | THR94 | |
| A | ARG98 | |
| A | GLU129 | |
| A | ASP154 | |
| A | ASN212 | |
| A | ARG230 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1af7 |
| Chain | Residue | Details |
| A | ARG98 | |
| A | ASP154 | |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 392 |
| Chain | Residue | Details |
| A | ARG53 | electrostatic stabiliser |
| A | ASP154 | activator |
