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 | 22 |
Details | binding site for residue SAH A 301 |
Chain | Residue |
A | SME40 |
A | GLU90 |
A | ILE91 |
A | GLY117 |
A | ALA118 |
A | SER119 |
A | GLN120 |
A | ASP141 |
A | HIS142 |
A | TRP143 |
A | ARG146 |
A | ASN41 |
A | HOH445 |
A | HOH484 |
A | HOH555 |
A | VAL42 |
A | GLY66 |
A | ALA67 |
A | TYR68 |
A | TYR71 |
A | SER72 |
A | MET89 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue 7JR A 302 |
Chain | Residue |
A | SME40 |
A | ALA97 |
A | GLN101 |
A | ASP141 |
A | LYS144 |
A | ASP169 |
A | ASN170 |
A | GLU199 |
A | SO4309 |
A | MG310 |
A | HOH442 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue CL A 303 |
Chain | Residue |
A | ASP44 |
A | ALA45 |
A | TYR200 |
A | HOH578 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue CXS A 304 |
Chain | Residue |
A | LYS5 |
A | TRP38 |
A | GLN100 |
A | ILE114 |
A | MET201 |
A | SO4308 |
A | HOH458 |
A | HOH459 |
A | HOH543 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue CXS A 305 |
Chain | Residue |
A | GLU155 |
A | TYR182 |
A | SER188 |
A | LYS202 |
A | PRO215 |
A | HOH408 |
A | HOH437 |
A | HOH471 |
A | HOH478 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue CXS A 306 |
Chain | Residue |
A | ARG8 |
A | LYS36 |
A | GLU37 |
A | HOH451 |
A | HOH566 |
A | HOH601 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue SO4 A 307 |
Chain | Residue |
A | GLY83 |
A | ARG85 |
A | LYS111 |
A | LYS128 |
A | HOH413 |
A | HOH425 |
A | HOH564 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue SO4 A 308 |
Chain | Residue |
A | GLU37 |
A | TRP38 |
A | LEU115 |
A | ASN116 |
A | CXS304 |
A | HOH414 |
A | HOH435 |
A | HOH467 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 309 |
Chain | Residue |
A | TRP143 |
A | LYS144 |
A | 7JR302 |
A | HOH401 |
A | HOH402 |
A | HOH585 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue MG A 310 |
Chain | Residue |
A | ASP141 |
A | ASP169 |
A | ASN170 |
A | 7JR302 |
A | HOH442 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | VAL42 | |
A | SER72 | |
A | GLU90 | |
A | ASP141 | |
Chain | Residue | Details |
A | GLU64 | |
A | ILE91 | |
A | SER119 | |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY117 | |
A | LYS144 | |
A | ASP169 | |
A | ASN170 | |
A | GLU199 | |
Chain | Residue | Details |
A | SER216 | |
A | SER217 | |
A | SER221 | |
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 |