6JCM
Crystal structure of ligand-free Rv0187.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| 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 | 0032259 | biological_process | methylation |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005886 | cellular_component | plasma membrane |
| 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 | 0032259 | biological_process | methylation |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005886 | cellular_component | plasma membrane |
| 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 | 0032259 | biological_process | methylation |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0008168 | molecular_function | methyltransferase activity |
| D | 0008171 | molecular_function | O-methyltransferase activity |
| D | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| D | 0016206 | molecular_function | catechol O-methyltransferase activity |
| D | 0032259 | biological_process | methylation |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 301 |
| Chain | Residue |
| A | GLN48 |
| A | ASP165 |
| A | PHE214 |
| A | HOH412 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ACT B 301 |
| Chain | Residue |
| B | GLN48 |
| B | ASP165 |
| B | PHE214 |
| B | HOH408 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ACT C 301 |
| Chain | Residue |
| C | ASP165 |
| C | PHE214 |
| C | HOH415 |
| C | GLN48 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue ACT D 301 |
| Chain | Residue |
| D | GLN48 |
| D | PHE137 |
| D | ASP165 |
| D | PHE214 |
| D | HOH425 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000305|PubMed:31147608 |
| Chain | Residue | Details |
| A | VAL44 | |
| B | GLU92 | |
| B | ALA121 | |
| B | ASP141 | |
| C | VAL44 | |
| C | GLY68 | |
| C | SER74 | |
| C | GLU92 | |
| C | ALA121 | |
| C | ASP141 | |
| D | VAL44 | |
| A | GLY68 | |
| D | GLY68 | |
| D | SER74 | |
| D | GLU92 | |
| D | ALA121 | |
| D | ASP141 | |
| A | SER74 | |
| A | GLU92 | |
| A | ALA121 | |
| A | ASP141 | |
| B | VAL44 | |
| B | GLY68 | |
| B | SER74 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019 |
| Chain | Residue | Details |
| A | GLU66 | |
| B | GLU66 | |
| C | GLU66 | |
| D | GLU66 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|PubMed:31147608 |
| Chain | Residue | Details |
| A | ASP139 | |
| D | ASP139 | |
| D | ASP165 | |
| D | ASN166 | |
| A | ASP165 | |
| A | ASN166 | |
| B | ASP139 | |
| B | ASP165 | |
| B | ASN166 | |
| C | ASP139 | |
| C | ASP165 | |
| C | ASN166 |
