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 | 28 |
Details | binding site for residue 619 A 301 |
Chain | Residue |
A | MET40 |
A | SER119 |
A | GLN120 |
A | ASP141 |
A | HIS142 |
A | TRP143 |
A | LYS144 |
A | ARG146 |
A | ASP169 |
A | ASN170 |
A | GLU199 |
A | GLY66 |
A | MG302 |
A | HOH414 |
A | HOH423 |
A | HOH450 |
A | HOH534 |
B | TRP38 |
B | LEU198 |
B | MET201 |
B | 619301 |
A | TYR68 |
A | GLU90 |
A | MET91 |
A | ASN92 |
A | TYR95 |
A | GLY117 |
A | ALA118 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MG A 302 |
Chain | Residue |
A | ASP141 |
A | ASP169 |
A | ASN170 |
A | 619301 |
A | HOH423 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue CL A 303 |
Chain | Residue |
A | ASP44 |
A | ALA45 |
A | TYR200 |
site_id | AC4 |
Number of Residues | 1 |
Details | binding site for residue CL A 304 |
site_id | AC5 |
Number of Residues | 12 |
Details | binding site for residue BTB A 305 |
Chain | Residue |
A | CYS33 |
A | THR34 |
A | LYS36 |
A | TRP38 |
A | TYR200 |
A | HOH404 |
A | HOH411 |
B | TRP143 |
B | LYS144 |
B | ASP145 |
B | PRO174 |
B | 619301 |
site_id | AC6 |
Number of Residues | 29 |
Details | binding site for residue 619 B 301 |
Chain | Residue |
A | TRP38 |
A | LEU198 |
A | MET201 |
A | 619301 |
A | BTB305 |
B | MET40 |
B | GLY66 |
B | TYR68 |
B | GLU90 |
B | MET91 |
B | ASN92 |
B | TYR95 |
B | GLY117 |
B | ALA118 |
B | SER119 |
B | GLN120 |
B | ASP141 |
B | HIS142 |
B | TRP143 |
B | LYS144 |
B | ARG146 |
B | ASP169 |
B | ASN170 |
B | GLU199 |
B | MG302 |
B | CL303 |
B | HOH428 |
B | HOH498 |
B | HOH516 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue MG B 302 |
Chain | Residue |
B | ASP141 |
B | ASP169 |
B | ASN170 |
B | 619301 |
B | HOH428 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue CL B 303 |
Chain | Residue |
A | GLU37 |
B | TRP143 |
B | 619301 |
B | HOH458 |
B | HOH498 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | VAL42 | |
A | SER72 | |
A | GLU90 | |
A | ASP141 | |
B | VAL42 | |
B | SER72 | |
B | GLU90 | |
B | ASP141 | |
Chain | Residue | Details |
A | GLU64 | |
A | MET91 | |
A | SER119 | |
B | GLU64 | |
B | MET91 | |
B | SER119 | |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY117 | |
B | GLU199 | |
A | LYS144 | |
A | ASP169 | |
A | ASN170 | |
A | GLU199 | |
B | GLY117 | |
B | LYS144 | |
B | ASP169 | |
B | ASN170 | |
Chain | Residue | Details |
A | SER216 | |
A | SER217 | |
A | SER221 | |
B | SER216 | |
B | SER217 | |
B | 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 |
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 |