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 | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 300 |
| Chain | Residue |
| A | ASP141 |
| A | ASP169 |
| A | ASN170 |
| A | CL4301 |
| A | HOH302 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE CL4 A 301 |
| Chain | Residue |
| A | MET89 |
| A | GLU90 |
| A | MET91 |
| A | ASN92 |
| A | TYR95 |
| A | GLY117 |
| A | ALA118 |
| A | SER119 |
| A | GLN120 |
| A | ASP141 |
| A | HIS142 |
| A | TRP143 |
| A | LYS144 |
| A | ASP169 |
| A | ASN170 |
| A | PRO174 |
| A | LEU198 |
| A | GLU199 |
| A | MG300 |
| A | HOH302 |
| A | HOH309 |
| A | TRP38 |
| A | MET40 |
| A | GLY66 |
| A | TYR68 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | VAL42 | |
| A | SER72 | |
| A | GLU90 | |
| A | ASP141 | |
| Chain | Residue | Details |
| A | GLU64 | |
| A | MET91 | |
| A | SER119 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY117 | |
| A | LYS144 | |
| A | ASP169 | |
| A | ASN170 | |
| A | GLU199 | |
| Chain | Residue | Details |
| A | SER216 | |
| A | SER217 | |
| A | SER221 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1vid |
| Chain | Residue | Details |
| A | GLU199 | |
| A | LYS144 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 915 |
| Chain | Residue | Details |
| A | ASP141 | metal ligand |
| A | LYS144 | proton shuttle (general acid/base) |
| A | ASP169 | metal ligand |
| A | ASN170 | metal ligand |
| A | GLU199 | electrostatic stabiliser |
