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 301 |
| Chain | Residue |
| A | ASP141 |
| A | ASP169 |
| A | ASN170 |
| A | 77P304 |
| A | HOH429 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| A | ASN41 |
| A | VAL42 |
| A | SER72 |
| A | HOH460 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 303 |
| Chain | Residue |
| A | ASP44 |
| A | ALA45 |
| A | TYR200 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue 77P A 304 |
| Chain | Residue |
| A | MET40 |
| A | MET91 |
| A | ASN92 |
| A | ALA97 |
| A | GLN100 |
| A | GLN101 |
| A | ASP141 |
| A | HIS142 |
| A | TRP143 |
| A | LYS144 |
| A | ASP169 |
| A | ASN170 |
| A | GLU199 |
| A | MG301 |
| A | HOH429 |
| A | HOH462 |
| A | HOH486 |
| A | HOH499 |
| A | HOH500 |
| A | HOH520 |
| A | HOH555 |
| A | HOH558 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 305 |
| Chain | Residue |
| A | GLY83 |
| A | ARG85 |
| A | LYS111 |
| A | LYS128 |
| A | HOH407 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue NHE A 306 |
| Chain | Residue |
| A | LYS5 |
| A | GLU37 |
| A | TRP38 |
| A | ALA96 |
| A | GLN100 |
| A | ILE114 |
| A | LEU115 |
| A | MET201 |
| A | HOH416 |
| A | HOH447 |
| A | HOH591 |
| A | HOH616 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue NHE A 307 |
| Chain | Residue |
| A | GLU155 |
| A | TYR182 |
| A | SER188 |
| A | PHE189 |
| A | TYR197 |
| A | PRO215 |
| A | SER216 |
| A | HOH410 |
| A | HOH426 |
| A | HOH428 |
| A | HOH438 |
| A | HOH441 |
| A | HOH448 |
| A | HOH625 |
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: {} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]} |
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 |
