5P8W
Crystal Structure of COMT in complex with [5-(2,4-dimethyl-1,3-thiazol-5-yl)-1H-pyrazol-3-yl]methanamine
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 |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0006584 | biological_process | catecholamine metabolic process |
| C | 0008171 | molecular_function | O-methyltransferase activity |
| C | 0016206 | molecular_function | catechol O-methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue DTT A 301 |
| Chain | Residue |
| A | LYS5 |
| A | ILE9 |
| A | CYS33 |
| A | TRP38 |
| A | ALA39 |
| A | MET40 |
| A | ASN41 |
| A | CYS69 |
| A | HOH415 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue O01 A 302 |
| Chain | Residue |
| A | GLY66 |
| A | TYR68 |
| A | MET89 |
| A | GLU90 |
| A | ILE91 |
| A | GLY117 |
| A | ALA118 |
| A | SER119 |
| A | GLN120 |
| A | HIS142 |
| A | TRP143 |
| A | ARG146 |
| C | HOH403 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue FMT A 303 |
| Chain | Residue |
| A | THR176 |
| A | PRO177 |
| A | ASP178 |
| A | PHE179 |
| A | HOH439 |
| A | HOH466 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 304 |
| Chain | Residue |
| A | ASN41 |
| A | ASP141 |
| A | ASP169 |
| A | ASN170 |
| A | HOH472 |
| A | HOH489 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue NA A 305 |
| Chain | Residue |
| A | VAL183 |
| A | ARG184 |
| A | SER186 |
| A | PHE189 |
| A | TYR197 |
| A | HOH401 |
| A | HOH531 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue DTT B 301 |
| Chain | Residue |
| B | ILE9 |
| B | CYS33 |
| B | ALA39 |
| B | MET40 |
| B | CYS69 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue O01 B 302 |
| Chain | Residue |
| B | GLY66 |
| B | TYR68 |
| B | MET89 |
| B | GLU90 |
| B | ILE91 |
| B | GLY117 |
| B | ALA118 |
| B | SER119 |
| B | GLN120 |
| B | HIS142 |
| B | TRP143 |
| B | ARG146 |
| B | HOH409 |
| B | HOH437 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue FMT B 303 |
| Chain | Residue |
| B | THR176 |
| B | PRO177 |
| B | ASP178 |
| B | PHE179 |
| B | HOH423 |
| B | HOH424 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 304 |
| Chain | Residue |
| B | VAL183 |
| B | ARG184 |
| B | SER186 |
| B | PHE189 |
| B | HOH489 |
| B | HOH496 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue NA B 305 |
| Chain | Residue |
| B | CYS33 |
| B | LYS36 |
| B | ALA39 |
| B | ASN41 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue DTT C 301 |
| Chain | Residue |
| C | ILE9 |
| C | CYS33 |
| C | TYR68 |
| C | CYS69 |
| site_id | AD3 |
| Number of Residues | 12 |
| Details | binding site for residue O01 C 302 |
| Chain | Residue |
| A | VAL204 |
| B | TYR197 |
| C | GLY66 |
| C | GLU90 |
| C | ILE91 |
| C | GLY117 |
| C | ALA118 |
| C | SER119 |
| C | GLN120 |
| C | HIS142 |
| C | HOH414 |
| C | HOH415 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue FMT C 303 |
| Chain | Residue |
| C | LYS144 |
| C | ASN170 |
| C | ILE172 |
| C | VAL173 |
| C | PRO174 |
| C | GLY175 |
| C | HOH436 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue NA C 304 |
| Chain | Residue |
| C | VAL183 |
| C | ARG184 |
| C | SER186 |
| C | PHE189 |
| C | GLU199 |
| C | HOH411 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|PubMed:12237326 |
| Chain | Residue | Details |
| C | SER72 | |
| C | GLU90 | |
| C | ASP141 | |
| A | VAL42 | |
| A | SER72 | |
| A | GLU90 | |
| A | ASP141 | |
| B | VAL42 | |
| B | SER72 | |
| B | GLU90 | |
| B | ASP141 | |
| C | VAL42 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019 |
| Chain | Residue | Details |
| B | GLU64 | |
| B | ILE91 | |
| B | SER119 | |
| C | GLU64 | |
| C | ILE91 | |
| C | SER119 | |
| A | ILE91 | |
| A | SER119 | |
| A | GLU64 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 15 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN170 | |
| A | GLU199 | |
| B | GLY117 | |
| B | LYS144 | |
| B | ASP169 | |
| B | ASN170 | |
| B | GLU199 | |
| C | GLY117 | |
| C | LYS144 | |
| C | ASP169 | |
| C | ASN170 | |
| C | GLU199 | |
| A | LYS144 | |
| A | ASP169 | |
| A | GLY117 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 9 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| A | SER216 | |
| A | SER217 | |
| A | SER221 | |
| B | SER217 | |
| B | SER221 | |
| C | SER216 | |
| C | SER217 | |
| C | SER221 | |
| B | SER216 |
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 |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 915 |
| Chain | Residue | Details |
| C | ASP141 | metal ligand |
| C | LYS144 | proton shuttle (general acid/base) |
| C | ASP169 | metal ligand |
| C | ASN170 | metal ligand |
| C | GLU199 | electrostatic stabiliser |
