6JCL
Crystal structure of cofactor-bound Rv0187 from MTB
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 | 0016740 | molecular_function | transferase 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 | 0016740 | molecular_function | transferase 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 | 0016740 | molecular_function | transferase 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 | 0016740 | molecular_function | transferase activity |
| D | 0032259 | biological_process | methylation |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0008168 | molecular_function | methyltransferase activity |
| E | 0008171 | molecular_function | O-methyltransferase activity |
| E | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| E | 0016206 | molecular_function | catechol O-methyltransferase activity |
| E | 0016740 | molecular_function | transferase activity |
| E | 0032259 | biological_process | methylation |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0008168 | molecular_function | methyltransferase activity |
| F | 0008171 | molecular_function | O-methyltransferase activity |
| F | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| F | 0016206 | molecular_function | catechol O-methyltransferase activity |
| F | 0016740 | molecular_function | transferase activity |
| F | 0032259 | biological_process | methylation |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0005886 | cellular_component | plasma membrane |
| G | 0008168 | molecular_function | methyltransferase activity |
| G | 0008171 | molecular_function | O-methyltransferase activity |
| G | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| G | 0016206 | molecular_function | catechol O-methyltransferase activity |
| G | 0016740 | molecular_function | transferase activity |
| G | 0032259 | biological_process | methylation |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0005886 | cellular_component | plasma membrane |
| H | 0008168 | molecular_function | methyltransferase activity |
| H | 0008171 | molecular_function | O-methyltransferase activity |
| H | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| H | 0016206 | molecular_function | catechol O-methyltransferase activity |
| H | 0016740 | molecular_function | transferase activity |
| H | 0032259 | biological_process | methylation |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue SAH A 301 |
| Chain | Residue |
| A | ALA43 |
| A | GLN94 |
| A | HIS97 |
| A | GLY119 |
| A | PRO120 |
| A | ALA121 |
| A | ASP139 |
| A | ALA140 |
| A | ASP141 |
| A | TYR148 |
| A | HOH431 |
| A | VAL44 |
| A | HOH438 |
| A | HOH464 |
| A | HOH473 |
| A | HOH487 |
| C | HOH476 |
| A | GLY68 |
| A | THR69 |
| A | LEU70 |
| A | PHE73 |
| A | SER74 |
| A | GLU92 |
| A | TYR93 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue SR A 302 |
| Chain | Residue |
| A | ASP139 |
| A | ASP165 |
| A | ASN166 |
| A | HOH438 |
| C | ASP178 |
| C | HOH444 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue MPD A 303 |
| Chain | Residue |
| A | VAL44 |
| A | GLN48 |
| A | PHE51 |
| A | LEU52 |
| A | VAL163 |
| A | ASP165 |
| A | PHE214 |
| A | HOH428 |
| A | HOH443 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue SR A 304 |
| Chain | Residue |
| A | ASP179 |
| A | ASP181 |
| C | ASP179 |
| C | ASP181 |
| C | HOH421 |
| C | HOH508 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue SR A 305 |
| Chain | Residue |
| A | ASP178 |
| A | HOH475 |
| C | ASP139 |
| C | ASP165 |
| C | ASN166 |
| C | HOH424 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | binding site for residue SAH B 301 |
| Chain | Residue |
| B | ALA43 |
| B | VAL44 |
| B | GLY68 |
| B | THR69 |
| B | LEU70 |
| B | PHE73 |
| B | SER74 |
| B | GLU92 |
| B | TYR93 |
| B | GLN94 |
| B | HIS97 |
| B | PRO120 |
| B | ALA121 |
| B | ASP139 |
| B | ALA140 |
| B | ASP141 |
| B | TYR148 |
| B | HOH450 |
| B | HOH464 |
| B | HOH466 |
| B | HOH479 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue SR B 302 |
| Chain | Residue |
| B | ASP139 |
| B | ASP165 |
| B | ASN166 |
| B | HOH450 |
| E | ASP178 |
| E | HOH417 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue MPD B 303 |
| Chain | Residue |
| A | ILE203 |
| B | VAL44 |
| B | GLN48 |
| B | LEU52 |
| B | VAL163 |
| B | ASP165 |
| B | PHE214 |
| B | HOH424 |
| B | HOH451 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue MPD B 304 |
| Chain | Residue |
| A | GLN106 |
| B | GLN150 |
| B | TRP151 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 305 |
| Chain | Residue |
| B | MET192 |
| B | GLY193 |
| B | HIS195 |
| B | LEU198 |
| B | HOH401 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue SR B 306 |
| Chain | Residue |
| E | ASN166 |
| E | HOH439 |
| B | ASP178 |
| B | HOH433 |
| E | ASP139 |
| E | ASP165 |
| site_id | AD3 |
| Number of Residues | 21 |
| Details | binding site for residue SAH C 301 |
| Chain | Residue |
| A | GLU143 |
| C | ALA43 |
| C | VAL44 |
| C | GLY68 |
| C | LEU70 |
| C | PHE73 |
| C | SER74 |
| C | GLU92 |
| C | TYR93 |
| C | GLN94 |
| C | HIS97 |
| C | ALA121 |
| C | ASP139 |
| C | ALA140 |
| C | ASP141 |
| C | TYR148 |
| C | HOH424 |
| C | HOH434 |
| C | HOH447 |
| C | HOH453 |
| C | HOH492 |
| site_id | AD4 |
| Number of Residues | 10 |
| Details | binding site for residue MPD C 302 |
| Chain | Residue |
| C | VAL44 |
| C | GLN48 |
| C | PHE51 |
| C | LEU52 |
| C | VAL163 |
| C | ASP165 |
| C | PHE214 |
| C | HOH428 |
| C | HOH443 |
| D | ILE203 |
| site_id | AD5 |
| Number of Residues | 20 |
| Details | binding site for residue SAH D 301 |
| Chain | Residue |
| D | ILE42 |
| D | ALA43 |
| D | VAL44 |
| D | GLY68 |
| D | THR69 |
| D | LEU70 |
| D | PHE73 |
| D | SER74 |
| D | GLU92 |
| D | TYR93 |
| D | GLN94 |
| D | HIS97 |
| D | ALA121 |
| D | ASP139 |
| D | ALA140 |
| D | ASP141 |
| D | TYR148 |
| D | HOH430 |
| D | HOH449 |
| D | HOH456 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue SR D 302 |
| Chain | Residue |
| D | ASP139 |
| D | ASP165 |
| D | ASN166 |
| D | HOH430 |
| H | ASP178 |
| H | HOH427 |
| site_id | AD7 |
| Number of Residues | 10 |
| Details | binding site for residue MPD D 303 |
| Chain | Residue |
| C | ILE203 |
| D | VAL44 |
| D | GLN48 |
| D | PHE51 |
| D | PHE137 |
| D | VAL163 |
| D | ASP165 |
| D | PHE214 |
| D | HOH428 |
| D | HOH463 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue SR D 304 |
| Chain | Residue |
| D | ASP178 |
| D | HOH406 |
| H | ASP139 |
| H | ASP165 |
| H | ASN166 |
| H | HOH433 |
| site_id | AD9 |
| Number of Residues | 19 |
| Details | binding site for residue SAH G 301 |
| Chain | Residue |
| G | ALA43 |
| G | VAL44 |
| G | GLY68 |
| G | THR69 |
| G | LEU70 |
| G | PHE73 |
| G | SER74 |
| G | GLU92 |
| G | TYR93 |
| G | HIS97 |
| G | ALA121 |
| G | ASP139 |
| G | ALA140 |
| G | ASP141 |
| G | TYR148 |
| G | HOH422 |
| G | HOH426 |
| G | HOH441 |
| G | HOH450 |
| site_id | AE1 |
| Number of Residues | 6 |
| Details | binding site for residue SR G 302 |
| Chain | Residue |
| F | ASP178 |
| F | HOH415 |
| G | ASP139 |
| G | ASP165 |
| G | ASN166 |
| G | HOH426 |
| site_id | AE2 |
| Number of Residues | 11 |
| Details | binding site for residue MPD G 303 |
| Chain | Residue |
| G | VAL44 |
| G | GLN48 |
| G | PHE51 |
| G | LEU52 |
| G | PHE137 |
| G | VAL163 |
| G | ASP165 |
| G | PHE214 |
| G | HOH432 |
| G | HOH435 |
| H | ILE203 |
| site_id | AE3 |
| Number of Residues | 6 |
| Details | binding site for residue SR G 304 |
| Chain | Residue |
| F | ASP179 |
| F | ASP181 |
| F | HOH482 |
| G | ASP179 |
| G | ASP181 |
| G | HOH445 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue SR G 305 |
| Chain | Residue |
| F | ASP139 |
| F | ASP165 |
| F | ASN166 |
| F | HOH413 |
| G | ASP178 |
| G | HOH423 |
| site_id | AE5 |
| Number of Residues | 19 |
| Details | binding site for residue SAH H 301 |
| Chain | Residue |
| H | ALA43 |
| H | VAL44 |
| H | GLY68 |
| H | THR69 |
| H | LEU70 |
| H | PHE73 |
| H | SER74 |
| H | GLU92 |
| H | TYR93 |
| H | HIS97 |
| H | GLY119 |
| H | PRO120 |
| H | ALA121 |
| H | ASP139 |
| H | ALA140 |
| H | ASP141 |
| H | TYR148 |
| H | HOH424 |
| H | HOH433 |
| site_id | AE6 |
| Number of Residues | 8 |
| Details | binding site for residue MPD H 302 |
| Chain | Residue |
| G | ILE203 |
| H | GLN48 |
| H | PHE137 |
| H | VAL163 |
| H | ASP165 |
| H | PHE214 |
| H | HOH405 |
| H | HOH453 |
| site_id | AE7 |
| Number of Residues | 20 |
| Details | binding site for residue SAH E 301 |
| Chain | Residue |
| E | ALA43 |
| E | VAL44 |
| E | GLY68 |
| E | LEU70 |
| E | PHE73 |
| E | SER74 |
| E | GLU92 |
| E | TYR93 |
| E | GLN94 |
| E | HIS97 |
| E | GLY119 |
| E | PRO120 |
| E | ALA121 |
| E | ASP139 |
| E | ALA140 |
| E | ASP141 |
| E | TYR148 |
| E | HOH439 |
| E | HOH455 |
| E | HOH477 |
| site_id | AE8 |
| Number of Residues | 6 |
| Details | binding site for residue MPD E 302 |
| Chain | Residue |
| E | GLN48 |
| E | ASP165 |
| E | PHE214 |
| E | HOH423 |
| E | HOH473 |
| F | ILE203 |
| site_id | AE9 |
| Number of Residues | 24 |
| Details | binding site for residue SAH F 301 |
| Chain | Residue |
| F | ILE42 |
| F | ALA43 |
| F | VAL44 |
| F | GLY68 |
| F | THR69 |
| F | LEU70 |
| F | PHE73 |
| F | SER74 |
| F | GLU92 |
| F | TYR93 |
| F | GLN94 |
| F | HIS97 |
| F | GLY119 |
| F | PRO120 |
| F | ALA121 |
| F | ASP139 |
| F | ALA140 |
| F | ASP141 |
| F | TYR148 |
| F | HOH413 |
| F | HOH441 |
| F | HOH453 |
| F | HOH481 |
| G | GLU143 |
| site_id | AF1 |
| Number of Residues | 10 |
| Details | binding site for residue MPD F 302 |
| Chain | Residue |
| E | ILE203 |
| F | VAL44 |
| F | GLN48 |
| F | PHE51 |
| F | LEU52 |
| F | VAL163 |
| F | ASP165 |
| F | PHE214 |
| F | HOH421 |
| F | HOH439 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31147608","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31147608","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






