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 | 18 |
| Details | BINDING SITE FOR RESIDUE SAH A 301 |
| Chain | Residue |
| A | LYS89 |
| A | ALA161 |
| A | SER162 |
| A | GLN163 |
| A | ASP184 |
| A | HIS185 |
| A | TRP186 |
| A | ARG189 |
| A | HOH410 |
| A | HOH416 |
| A | GLY109 |
| A | ALA110 |
| A | TYR111 |
| A | TYR114 |
| A | SER115 |
| A | GLU133 |
| A | ILE134 |
| A | GLY160 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 302 |
| Chain | Residue |
| A | VAL226 |
| A | ARG227 |
| A | SER229 |
| A | PHE232 |
| A | HOH411 |
| A | HOH440 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SAH B 301 |
| Chain | Residue |
| B | ASN84 |
| B | VAL85 |
| B | GLY109 |
| B | ALA110 |
| B | TYR111 |
| B | TYR114 |
| B | SER115 |
| B | GLU133 |
| B | ILE134 |
| B | GLY160 |
| B | ALA161 |
| B | SER162 |
| B | GLN163 |
| B | ASP184 |
| B | HIS185 |
| B | TRP186 |
| B | HOH401 |
| B | HOH432 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 302 |
| Chain | Residue |
| B | ASP184 |
| B | ASP212 |
| B | ASN213 |
| B | HOH431 |
| B | HOH432 |
| B | HOH441 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| 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 | 6 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| 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 |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 915 |
| Chain | Residue | Details |
| B | ASP184 | metal ligand |
| B | LYS187 | proton shuttle (general acid/base) |
| B | ASP212 | metal ligand |
| B | ASN213 | metal ligand |
| B | GLU242 | electrostatic stabiliser |
