Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0006584 | biological_process | catecholamine metabolic process |
| A | 0008171 | molecular_function | O-methyltransferase activity |
| A | 0016206 | molecular_function | catechol O-methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE 542 A 1 |
| Chain | Residue |
| A | CXS3 |
| A | ALA140 |
| A | GLN143 |
| A | GLN144 |
| A | GLY160 |
| A | ALA161 |
| A | SER162 |
| A | GLN163 |
| A | ASP184 |
| A | HIS185 |
| A | TRP186 |
| A | HOH43 |
| A | LYS187 |
| A | ARG189 |
| A | ASP212 |
| A | ASN213 |
| A | VAL216 |
| A | PRO217 |
| A | LEU241 |
| A | GLU242 |
| A | MG265 |
| A | HOH332 |
| A | MET83 |
| A | HOH337 |
| A | HOH369 |
| A | HOH379 |
| A | GLY109 |
| A | TYR111 |
| A | GLU133 |
| A | MET134 |
| A | ASN135 |
| A | TYR138 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CXS A 3 |
| Chain | Residue |
| A | 5421 |
| A | HOH29 |
| A | LYS48 |
| A | TRP81 |
| A | ALA139 |
| A | ALA140 |
| A | GLN143 |
| A | ILE157 |
| A | MET244 |
| A | SO4270 |
| A | HOH398 |
| A | HOH401 |
| A | HOH471 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CXS A 2 |
| Chain | Residue |
| A | LEU195 |
| A | GLU198 |
| A | TYR225 |
| A | SER231 |
| A | PHE232 |
| A | TYR240 |
| A | LYS245 |
| A | PRO258 |
| A | HOH417 |
| A | HOH429 |
| A | HOH512 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 265 |
| Chain | Residue |
| A | 5421 |
| A | ASP184 |
| A | ASP212 |
| A | ASN213 |
| A | HOH369 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL A 266 |
| Chain | Residue |
| A | SER101 |
| A | SER103 |
| A | HOH294 |
| A | HOH344 |
| A | HOH371 |
| A | HOH454 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL A 267 |
| Chain | Residue |
| A | VAL226 |
| A | ARG227 |
| A | SER229 |
| A | PHE232 |
| A | HOH291 |
| A | HOH509 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 268 |
| Chain | Residue |
| A | ASP87 |
| A | ALA88 |
| A | TYR243 |
| A | HOH361 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 269 |
| Chain | Residue |
| A | PRO125 |
| A | GLY126 |
| A | ARG128 |
| A | LYS154 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 270 |
| Chain | Residue |
| A | CXS3 |
| A | TRP81 |
| A | LEU158 |
| A | ASN159 |
| A | MET244 |
| A | HOH313 |
| A | HOH384 |
| A | HOH511 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12237326","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1vid |
| Chain | Residue | Details |
| A | LYS187 | |
| A | GLU242 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 915 |
| Chain | Residue | Details |
| A | ASP184 | metal ligand |
| A | LYS187 | proton shuttle (general acid/base) |
| A | ASP212 | metal ligand |
| A | ASN213 | metal ligand |
| A | GLU242 | electrostatic stabiliser |
