7CVV
Crystal structure of Catechol o-methyl transferase (COMT) from Niastella koreensis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008171 | molecular_function | O-methyltransferase activity |
| A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| A | 0016206 | molecular_function | catechol O-methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0032259 | biological_process | methylation |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008171 | molecular_function | O-methyltransferase activity |
| B | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| B | 0016206 | molecular_function | catechol O-methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0008171 | molecular_function | O-methyltransferase activity |
| C | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| C | 0016206 | molecular_function | catechol O-methyltransferase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0032259 | biological_process | methylation |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue SAM A 301 |
| Chain | Residue |
| A | ILE39 |
| A | TYR90 |
| A | HIS94 |
| A | ALA118 |
| A | ASP139 |
| A | ASP141 |
| A | TYR148 |
| A | SER40 |
| A | VAL41 |
| A | GLY65 |
| A | THR66 |
| A | LEU67 |
| A | TYR70 |
| A | SER71 |
| A | GLU89 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residue SAM B 301 |
| Chain | Residue |
| B | ILE39 |
| B | SER40 |
| B | VAL41 |
| B | GLU63 |
| B | GLY65 |
| B | THR66 |
| B | LEU67 |
| B | TYR70 |
| B | SER71 |
| B | GLU89 |
| B | TYR90 |
| B | HIS94 |
| B | LYS117 |
| B | ALA118 |
| B | ASP139 |
| B | ASP141 |
| B | TYR148 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue SAM C 301 |
| Chain | Residue |
| C | ILE39 |
| C | SER40 |
| C | VAL41 |
| C | GLY65 |
| C | THR66 |
| C | LEU67 |
| C | SER71 |
| C | GLU89 |
| C | TYR90 |
| C | HIS94 |
| C | ALA118 |
| C | ASP139 |
| C | ASP141 |
| C | TYR148 |
| C | HOH403 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33596655","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CVV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CVW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CVX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33596655","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7CVW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CVX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33596655","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CVV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CVX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33596655","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CVW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CVX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
