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 |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0006584 | biological_process | catecholamine metabolic process |
| B | 0008171 | molecular_function | O-methyltransferase activity |
| B | 0016206 | molecular_function | catechol O-methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue SAH A 300 |
| Chain | Residue |
| A | MET40 |
| A | ILE91 |
| A | CYS95 |
| A | GLY117 |
| A | ALA118 |
| A | SER119 |
| A | ASP141 |
| A | HIS142 |
| A | TRP143 |
| A | 7JX302 |
| A | HOH408 |
| A | VAL42 |
| A | GLY66 |
| A | ALA67 |
| A | TYR68 |
| A | TYR71 |
| A | SER72 |
| A | MET89 |
| A | GLU90 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 301 |
| Chain | Residue |
| A | ASP141 |
| A | ASP169 |
| A | ASN170 |
| A | 7JX302 |
| A | HOH412 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue 7JX A 302 |
| Chain | Residue |
| A | ASP141 |
| A | HIS142 |
| A | LYS144 |
| A | ASP169 |
| A | ASN170 |
| A | SAH300 |
| A | MG301 |
| A | HOH402 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 303 |
| Chain | Residue |
| A | VAL183 |
| A | ARG184 |
| A | SER186 |
| A | PHE189 |
| A | HOH437 |
| A | HOH441 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | binding site for residue SAH B 301 |
| Chain | Residue |
| B | LYS46 |
| B | GLY66 |
| B | ALA67 |
| B | TYR68 |
| B | TYR71 |
| B | SER72 |
| B | GLU90 |
| B | ILE91 |
| B | GLY117 |
| B | ALA118 |
| B | SER119 |
| B | GLN120 |
| B | ASP141 |
| B | TRP143 |
| B | ARG146 |
| B | HOH401 |
| B | HOH414 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 302 |
| Chain | Residue |
| B | VAL183 |
| B | ARG184 |
| B | SER186 |
| B | PHE189 |
| B | HOH440 |
| B | HOH442 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | VAL42 | |
| A | SER72 | |
| A | GLU90 | |
| A | ASP141 | |
| B | VAL42 | |
| B | SER72 | |
| B | GLU90 | |
| B | ASP141 | |
| Chain | Residue | Details |
| A | GLU64 | |
| A | ILE91 | |
| A | SER119 | |
| B | GLU64 | |
| B | ILE91 | |
| B | SER119 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY117 | |
| B | GLU199 | |
| A | LYS144 | |
| A | ASP169 | |
| A | ASN170 | |
| A | GLU199 | |
| B | GLY117 | |
| B | LYS144 | |
| B | ASP169 | |
| B | ASN170 | |
| Chain | Residue | Details |
| A | SER216 | |
| A | SER217 | |
| A | SER221 | |
| B | SER216 | |
| B | SER217 | |
| B | SER221 | |
Catalytic Information from CSA
| 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 |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 915 |
| Chain | Residue | Details |
| B | ASP141 | metal ligand |
| B | LYS144 | proton shuttle (general acid/base) |
| B | ASP169 | metal ligand |
| B | ASN170 | metal ligand |
| B | GLU199 | electrostatic stabiliser |
