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 | 23 |
Details | binding site for residue SAH A 301 |
Chain | Residue |
A | MET40 |
A | GLU90 |
A | ILE91 |
A | ASN92 |
A | GLY117 |
A | ALA118 |
A | SER119 |
A | GLN120 |
A | ASP141 |
A | HIS142 |
A | 7JV302 |
A | ASN41 |
A | HOH446 |
A | HOH448 |
A | HOH542 |
A | HOH550 |
A | VAL42 |
A | GLY66 |
A | ALA67 |
A | TYR68 |
A | TYR71 |
A | SER72 |
A | MET89 |
site_id | AC2 |
Number of Residues | 18 |
Details | binding site for residue 7JV A 302 |
Chain | Residue |
A | TRP38 |
A | MET40 |
A | ALA97 |
A | GLN101 |
A | ASN104 |
A | ASP141 |
A | HIS142 |
A | TRP143 |
A | ASP169 |
A | ASN170 |
A | PRO174 |
A | GLU199 |
A | SAH301 |
A | MG307 |
A | HOH407 |
A | HOH461 |
A | HOH511 |
A | HOH518 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue CL A 303 |
Chain | Residue |
A | ASP44 |
A | ALA45 |
A | TYR200 |
A | HOH590 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue D1D A 304 |
Chain | Residue |
A | TRP38 |
A | ALA97 |
A | GLN100 |
A | ASN116 |
A | MET201 |
A | HOH421 |
A | HOH467 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue K A 305 |
Chain | Residue |
A | VAL183 |
A | ARG184 |
A | SER186 |
A | PHE189 |
A | HOH564 |
A | HOH577 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue K A 306 |
Chain | Residue |
A | SER58 |
A | SER60 |
A | HOH500 |
A | HOH552 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue MG A 307 |
Chain | Residue |
A | ASP141 |
A | ASP169 |
A | ASN170 |
A | 7JV302 |
A | HOH461 |
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: {} |
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 |