6J24
Crystal structure of a SAM-dependent methyltransferase LepI in complex with its substrate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008171 | molecular_function | O-methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0032259 | biological_process | methylation |
| A | 0044550 | biological_process | secondary metabolite biosynthetic process |
| A | 0046983 | molecular_function | protein dimerization activity |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008171 | molecular_function | O-methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0044550 | biological_process | secondary metabolite biosynthetic process |
| B | 0046983 | molecular_function | protein dimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue BYO B 401 |
| Chain | Residue |
| B | HIS133 |
| B | LEU138 |
| B | ARG295 |
| B | ASP296 |
| B | THR338 |
| B | CYS341 |
| B | ALA345 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue SAM B 402 |
| Chain | Residue |
| B | ASP252 |
| B | LEU253 |
| B | VAL256 |
| B | HIS274 |
| B | ASN275 |
| B | PHE276 |
| B | HIS277 |
| B | ARG291 |
| B | LEU292 |
| B | ILE293 |
| B | HOH532 |
| B | HOH541 |
| B | GLY227 |
| B | GLY229 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue BYO A 401 |
| Chain | Residue |
| A | GLY130 |
| A | HIS133 |
| A | LEU138 |
| A | PHE189 |
| A | ALA345 |
| B | MET45 |
| B | SER48 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue SAM A 402 |
| Chain | Residue |
| A | GLY227 |
| A | GLY229 |
| A | ASP252 |
| A | LEU253 |
| A | VAL256 |
| A | HIS274 |
| A | ASN275 |
| A | PHE276 |
| A | HIS277 |
| A | ARG291 |
| A | LEU292 |
| A | HOH508 |
| A | HOH529 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | Region: {"description":"Substrate binding","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O04385","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01020","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
