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 | 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 |
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 | 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 | 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 | 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 | 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: 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 | |
G | VAL44 | |
G | GLY68 | |
G | SER74 | |
G | GLU92 | |
G | ALA121 | |
A | SER74 | |
G | ASP141 | |
H | VAL44 | |
H | GLY68 | |
H | SER74 | |
H | GLU92 | |
H | ALA121 | |
H | ASP141 | |
E | VAL44 | |
E | GLY68 | |
E | SER74 | |
A | GLU92 | |
E | GLU92 | |
E | ALA121 | |
E | ASP141 | |
F | VAL44 | |
F | GLY68 | |
F | SER74 | |
F | GLU92 | |
F | ALA121 | |
F | ASP141 | |
A | ALA121 | |
A | ASP141 | |
B | VAL44 | |
B | GLY68 | |
B | SER74 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019 |
Chain | Residue | Details |
A | GLU66 | |
B | GLU66 | |
C | GLU66 | |
D | GLU66 | |
G | GLU66 | |
H | GLU66 | |
E | GLU66 | |
F | GLU66 |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|PubMed:31147608 |
Chain | Residue | Details |
A | ASP139 | |
D | ASP139 | |
D | ASP165 | |
D | ASN166 | |
G | ASP139 | |
G | ASP165 | |
G | ASN166 | |
H | ASP139 | |
H | ASP165 | |
H | ASN166 | |
E | ASP139 | |
A | ASP165 | |
E | ASP165 | |
E | ASN166 | |
F | ASP139 | |
F | ASP165 | |
F | ASN166 | |
A | ASN166 | |
B | ASP139 | |
B | ASP165 | |
B | ASN166 | |
C | ASP139 | |
C | ASP165 | |
C | ASN166 |