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 | 25 |
| Details | binding site for residue SFG A 300 |
| Chain | Residue |
| A | LYS89 |
| A | GLY160 |
| A | ALA161 |
| A | SER162 |
| A | GLN163 |
| A | ASP184 |
| A | HIS185 |
| A | TRP186 |
| A | HOH461 |
| A | HOH509 |
| A | HOH524 |
| A | GLY109 |
| A | HOH588 |
| A | HOH647 |
| A | HOH672 |
| A | HOH673 |
| A | HOH678 |
| A | HOH694 |
| A | ALA110 |
| A | TYR111 |
| A | TYR114 |
| A | SER115 |
| A | GLU133 |
| A | MET134 |
| A | TYR138 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue TLA A 301 |
| Chain | Residue |
| A | ARG51 |
| A | ARG54 |
| A | TYR75 |
| A | LYS79 |
| A | LYS263 |
| A | HOH422 |
| A | HOH448 |
| A | HOH468 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue K A 302 |
| Chain | Residue |
| A | SER101 |
| A | SER103 |
| A | HOH402 |
| A | HOH408 |
| A | HOH614 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue K A 303 |
| Chain | Residue |
| A | ASP184 |
| A | HIS185 |
| A | TYR190 |
| A | ASN213 |
| A | HOH678 |
| A | HOH685 |
| A | HOH694 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue K A 304 |
| Chain | Residue |
| A | VAL226 |
| A | ARG227 |
| A | SER229 |
| A | PHE232 |
| A | HOH599 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 305 |
| Chain | Residue |
| A | ARG51 |
| A | LYS79 |
| A | TRP81 |
| A | HOH419 |
| A | HOH565 |
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 | 2 |
| 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 | ASP184 | metal ligand |
| A | LYS187 | proton shuttle (general acid/base) |
| A | ASP212 | metal ligand |
| A | ASN213 | metal ligand |
| A | GLU242 | electrostatic stabiliser |
