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 | 12 |
| Details | binding site for residue NHE A 301 |
| Chain | Residue |
| A | LYS5 |
| B | ASP145 |
| B | 6PM302 |
| B | HOH435 |
| A | GLU6 |
| A | TRP38 |
| A | ASN92 |
| A | CYS95 |
| A | 6PM302 |
| A | HOH465 |
| B | TRP143 |
| B | LYS144 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue 6PM A 302 |
| Chain | Residue |
| A | MET40 |
| A | GLY66 |
| A | MET89 |
| A | GLU90 |
| A | ILE91 |
| A | GLY117 |
| A | ALA118 |
| A | SER119 |
| A | GLN120 |
| A | HIS142 |
| A | TRP143 |
| A | ARG146 |
| A | NHE301 |
| B | 6PM302 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 303 |
| Chain | Residue |
| A | ASP141 |
| A | ASP169 |
| A | ASN170 |
| A | HOH483 |
| A | HOH495 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 304 |
| Chain | Residue |
| A | VAL183 |
| A | ARG184 |
| A | SER186 |
| A | PHE189 |
| A | HOH489 |
| A | HOH497 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue NHE B 301 |
| Chain | Residue |
| A | TRP143 |
| A | LYS144 |
| A | ASP145 |
| A | HOH428 |
| B | LYS5 |
| B | GLU6 |
| B | TRP38 |
| B | ASN92 |
| B | CYS95 |
| B | 6PM302 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for residue 6PM B 302 |
| Chain | Residue |
| A | NHE301 |
| A | 6PM302 |
| B | GLY66 |
| B | TYR68 |
| B | MET89 |
| B | GLU90 |
| B | ILE91 |
| B | GLY117 |
| B | ALA118 |
| B | SER119 |
| B | GLN120 |
| B | ASP141 |
| B | HIS142 |
| B | TRP143 |
| B | ARG146 |
| B | NHE301 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 303 |
| Chain | Residue |
| B | VAL183 |
| B | ARG184 |
| B | SER186 |
| B | PHE189 |
| B | HOH517 |
| B | HOH523 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 304 |
| Chain | Residue |
| B | ASP141 |
| B | ASP169 |
| B | ASN170 |
| B | HOH407 |
| B | HOH482 |
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 | 5 |
| 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 |
| 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 |
