5K0N
Crystal Structure of COMT in complex with 4-[5-[1-(4-methoxyphenyl)cyclopropyl]-1H-pyrazol-3-yl]-1,3-dimethylpyrazole
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 |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0006584 | biological_process | catecholamine metabolic process |
| D | 0008171 | molecular_function | O-methyltransferase activity |
| D | 0016206 | molecular_function | catechol O-methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 301 |
| Chain | Residue |
| A | ALA52 |
| A | VAL53 |
| A | GLU56 |
| A | TYR194 |
| A | LYS209 |
| B | SER195 |
| B | SER196 |
| B | TYR197 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | ASP141 |
| A | LYS144 |
| A | ASN170 |
| A | HOH402 |
| A | HOH422 |
| A | ASN41 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue NHE A 303 |
| Chain | Residue |
| A | LYS5 |
| A | GLU6 |
| A | ASN92 |
| A | HOH437 |
| A | HOH490 |
| C | TRP143 |
| C | LYS144 |
| C | ASP145 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue 6P0 A 304 |
| Chain | Residue |
| A | ASN41 |
| A | GLY66 |
| A | TYR68 |
| A | MET89 |
| A | GLU90 |
| A | ILE91 |
| A | GLY117 |
| A | ALA118 |
| A | SER119 |
| A | GLN120 |
| A | HIS142 |
| A | TRP143 |
| A | ARG146 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue K A 305 |
| Chain | Residue |
| A | VAL183 |
| A | ARG184 |
| A | SER186 |
| A | PHE189 |
| A | HOH493 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 301 |
| Chain | Residue |
| B | ASN41 |
| B | ASP141 |
| B | ASN170 |
| B | HOH402 |
| B | HOH419 |
| B | HOH516 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue NHE B 302 |
| Chain | Residue |
| B | TRP143 |
| B | LYS144 |
| B | ASP145 |
| B | 6P0303 |
| B | HOH442 |
| D | LYS5 |
| D | GLU6 |
| D | TRP38 |
| D | ASN92 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | binding site for residue 6P0 B 303 |
| Chain | Residue |
| B | ASN41 |
| 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 | NHE302 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue K B 304 |
| Chain | Residue |
| B | VAL183 |
| B | ARG184 |
| B | SER186 |
| B | PHE189 |
| B | HOH513 |
| B | HOH534 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 301 |
| Chain | Residue |
| C | ASN41 |
| C | ASP141 |
| C | ASN170 |
| C | NHE302 |
| C | HOH401 |
| C | HOH415 |
| site_id | AD2 |
| Number of Residues | 9 |
| Details | binding site for residue NHE C 302 |
| Chain | Residue |
| C | TRP38 |
| C | MET40 |
| C | ASN41 |
| C | ASN170 |
| C | TYR200 |
| C | MG301 |
| C | HOH401 |
| C | HOH411 |
| C | HOH433 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue NHE C 303 |
| Chain | Residue |
| A | TRP143 |
| A | LYS144 |
| A | ASP145 |
| C | LYS5 |
| C | GLU6 |
| C | TRP38 |
| C | ASN92 |
| C | HOH436 |
| site_id | AD4 |
| Number of Residues | 13 |
| Details | binding site for residue 6P0 C 304 |
| Chain | Residue |
| C | ASN41 |
| C | GLY66 |
| C | TYR68 |
| C | MET89 |
| C | GLU90 |
| C | ILE91 |
| C | GLY117 |
| C | ALA118 |
| C | SER119 |
| C | GLN120 |
| C | HIS142 |
| C | TRP143 |
| A | HOH490 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue K C 305 |
| Chain | Residue |
| C | VAL183 |
| C | ARG184 |
| C | SER186 |
| C | PHE189 |
| C | HOH519 |
| C | HOH522 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 301 |
| Chain | Residue |
| C | THR192 |
| D | ILE172 |
| D | ARG184 |
| D | HOH514 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 302 |
| Chain | Residue |
| D | ASN41 |
| D | ASP141 |
| D | ASN170 |
| D | NHE303 |
| D | HOH406 |
| D | HOH423 |
| site_id | AD8 |
| Number of Residues | 10 |
| Details | binding site for residue NHE D 303 |
| Chain | Residue |
| D | TRP38 |
| D | MET40 |
| D | ASN41 |
| D | ASN170 |
| D | LEU198 |
| D | TYR200 |
| D | MG302 |
| D | HOH406 |
| D | HOH426 |
| D | HOH490 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for residue NHE D 304 |
| Chain | Residue |
| B | LYS5 |
| B | GLU6 |
| B | ASN92 |
| B | HOH446 |
| D | LYS144 |
| D | ASP145 |
| D | HOH452 |
| site_id | AE1 |
| Number of Residues | 13 |
| Details | binding site for residue 6P0 D 305 |
| Chain | Residue |
| D | ASN41 |
| D | GLY66 |
| D | TYR68 |
| D | MET89 |
| D | GLU90 |
| D | ILE91 |
| D | GLY117 |
| D | ALA118 |
| D | SER119 |
| D | GLN120 |
| D | HIS142 |
| D | TRP143 |
| D | HOH452 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue K D 306 |
| Chain | Residue |
| D | VAL183 |
| D | ARG184 |
| D | SER186 |
| D | PHE189 |
| D | HOH517 |
| D | HOH546 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12237326","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
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 |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 915 |
| Chain | Residue | Details |
| D | ASP141 | metal ligand |
| D | LYS144 | proton shuttle (general acid/base) |
| D | ASP169 | metal ligand |
| D | ASN170 | metal ligand |
| D | GLU199 | electrostatic stabiliser |
