6IWT
Crystal structure of methyltransferase COMT-S in P. praeruptorum
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 | 0009411 | biological_process | response to UV |
| A | 0009805 | biological_process | coumarin biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030752 | molecular_function | 5-hydroxyfuranocoumarin 5-O-methyltransferase activity |
| A | 0030753 | molecular_function | 8-hydroxyfuranocoumarin 8-O-methyltransferase activity |
| A | 0032259 | biological_process | methylation |
| A | 0042542 | biological_process | response to hydrogen peroxide |
| A | 0046983 | molecular_function | protein dimerization activity |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008171 | molecular_function | O-methyltransferase activity |
| B | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| B | 0009411 | biological_process | response to UV |
| B | 0009805 | biological_process | coumarin biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030752 | molecular_function | 5-hydroxyfuranocoumarin 5-O-methyltransferase activity |
| B | 0030753 | molecular_function | 8-hydroxyfuranocoumarin 8-O-methyltransferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0042542 | biological_process | response to hydrogen peroxide |
| B | 0046983 | molecular_function | protein dimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 401 |
| Chain | Residue |
| A | MET131 |
| A | ASN132 |
| A | LEU137 |
| A | HIS324 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue PEG A 402 |
| Chain | Residue |
| A | GLY327 |
| A | ASP271 |
| A | TRP272 |
| A | SER273 |
| A | HIS276 |
| A | ASN325 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01020","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A166U5H3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P28002","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Determines the catalytic selectivity of hydroxyl groups in esculetin between the 6-hydroxyl and 7-hydroxyl groups","evidences":[{"source":"PubMed","id":"30934718","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
