5X1J
Vanillate/3-O-methylgallate O-demethylase, LigM, vanillate complex form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0032259 | biological_process | methylation |
| A | 0046274 | biological_process | lignin catabolic process |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0046274 | biological_process | lignin catabolic process |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0032259 | biological_process | methylation |
| C | 0046274 | biological_process | lignin catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue VNL A 501 |
| Chain | Residue |
| A | TYR31 |
| A | HOH811 |
| A | HIS60 |
| A | MET61 |
| A | ARG122 |
| A | TYR247 |
| A | ASN250 |
| A | TRP256 |
| A | PRO258 |
| A | HOH618 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | GLY289 |
| A | ASN371 |
| A | TYR372 |
| A | ASN376 |
| A | ASP378 |
| A | HOH625 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | LEU261 |
| A | TYR265 |
| A | TYR282 |
| A | GLY286 |
| A | ALA287 |
| A | ASN374 |
| A | THR375 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue TRS A 504 |
| Chain | Residue |
| A | GLY428 |
| A | GLY429 |
| A | THR430 |
| A | LYS432 |
| A | VAL435 |
| A | HOH672 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue VNL B 501 |
| Chain | Residue |
| B | TYR31 |
| B | HIS60 |
| B | ARG122 |
| B | TYR247 |
| B | ASN250 |
| B | TRP256 |
| B | PRO258 |
| B | HOH626 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| B | LEU261 |
| B | TYR265 |
| B | TYR282 |
| B | GLY286 |
| B | ALA287 |
| B | ASN374 |
| B | THR375 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | GLY289 |
| B | GLY290 |
| B | ASN371 |
| B | TYR372 |
| B | ASN376 |
| B | ASP378 |
| B | HOH643 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue TRS B 504 |
| Chain | Residue |
| B | GLY428 |
| B | THR430 |
| B | ARG431 |
| B | LYS432 |
| B | VAL435 |
| C | HOH706 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue VNL C 501 |
| Chain | Residue |
| C | TYR31 |
| C | HIS60 |
| C | MET61 |
| C | ARG122 |
| C | TYR247 |
| C | ASN250 |
| C | TRP256 |
| C | PRO258 |
| C | HOH627 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 502 |
| Chain | Residue |
| C | GLY289 |
| C | GLY290 |
| C | ASN371 |
| C | TYR372 |
| C | ASN376 |
| C | ASP378 |
| C | HOH611 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28429420","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Site: {"description":"Important for activity","evidences":[{"source":"PubMed","id":"28429420","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Site: {"description":"Important for activity","evidences":[{"source":"PubMed","id":"28373573","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28429420","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
