5JR3
Crystal structure of carminomycin-4-O-methyltransferase DnrK in complex with SAH and 4-methylumbelliferone
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008171 | molecular_function | O-methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0032259 | biological_process | methylation |
| A | 0046983 | molecular_function | protein dimerization activity |
| A | 1901771 | biological_process | daunorubicin biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008171 | molecular_function | O-methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0032259 | biological_process | methylation |
| B | 0046983 | molecular_function | protein dimerization activity |
| B | 1901771 | biological_process | daunorubicin biosynthetic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0008171 | molecular_function | O-methyltransferase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0032259 | biological_process | methylation |
| C | 0046983 | molecular_function | protein dimerization activity |
| C | 1901771 | biological_process | daunorubicin biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue SAH A 401 |
| Chain | Residue |
| A | TYR143 |
| A | SER252 |
| A | PHE253 |
| A | ASN257 |
| A | HOH550 |
| A | HOH569 |
| A | HOH604 |
| A | HOH611 |
| A | HOH614 |
| A | HOH670 |
| A | HOH693 |
| A | ARG153 |
| A | LEU160 |
| A | GLY187 |
| A | GLU210 |
| A | MET211 |
| A | GLY236 |
| A | ASP237 |
| A | PHE238 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue 4MU A 402 |
| Chain | Residue |
| A | PHE156 |
| A | PHE253 |
| A | LEU300 |
| A | ARG303 |
| A | HOH584 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | ARG115 |
| A | ARG149 |
| A | HOH559 |
| A | HOH580 |
| A | HOH623 |
| B | HIS261 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 404 |
| Chain | Residue |
| A | ARG57 |
| A | HOH502 |
| A | HOH503 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 405 |
| Chain | Residue |
| A | ARG219 |
| A | ASP232 |
| A | VAL233 |
| A | HOH541 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 406 |
| Chain | Residue |
| A | LYS52 |
| A | HOH711 |
| C | THR50 |
| C | LYS52 |
| C | ALA53 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | binding site for residue SAH B 401 |
| Chain | Residue |
| B | TYR143 |
| B | ARG153 |
| B | LEU160 |
| B | GLY187 |
| B | GLU210 |
| B | MET211 |
| B | GLY236 |
| B | ASP237 |
| B | PHE238 |
| B | SER252 |
| B | PHE253 |
| B | ASN257 |
| B | HOH522 |
| B | HOH559 |
| B | HOH605 |
| B | HOH619 |
| B | HOH629 |
| B | HOH633 |
| B | HOH683 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue 4MU B 402 |
| Chain | Residue |
| B | PHE156 |
| B | LEU300 |
| B | ARG303 |
| B | HOH606 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 403 |
| Chain | Residue |
| A | ARG61 |
| A | ARG131 |
| A | PRO259 |
| A | HIS261 |
| A | HOH643 |
| B | HOH502 |
| B | HOH519 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 404 |
| Chain | Residue |
| B | ARG115 |
| B | ARG149 |
| B | HOH521 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 405 |
| Chain | Residue |
| B | ARG61 |
| B | PRO62 |
| B | GLU63 |
| B | HOH541 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 406 |
| Chain | Residue |
| A | ARG128 |
| B | ARG131 |
| B | PRO259 |
| B | HIS261 |
| B | HOH543 |
| B | HOH607 |
| C | ARG61 |
| site_id | AD4 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 B 407 |
| Chain | Residue |
| B | HIS289 |
| B | THR314 |
| B | LYS317 |
| B | HOH511 |
| B | HOH594 |
| B | HOH693 |
| C | GLU63 |
| C | LEU66 |
| C | ARG70 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 408 |
| Chain | Residue |
| B | HOH618 |
| B | ARG219 |
| B | ASP232 |
| B | VAL233 |
| B | HOH504 |
| site_id | AD6 |
| Number of Residues | 17 |
| Details | binding site for residue SAH C 401 |
| Chain | Residue |
| C | TYR143 |
| C | ARG153 |
| C | LEU160 |
| C | GLY187 |
| C | GLU210 |
| C | MET211 |
| C | GLY236 |
| C | ASP237 |
| C | PHE238 |
| C | SER252 |
| C | PHE253 |
| C | ASN257 |
| C | TRP258 |
| C | HOH522 |
| C | HOH594 |
| C | HOH595 |
| C | HOH643 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue 4MU C 402 |
| Chain | Residue |
| C | PHE156 |
| C | LEU160 |
| C | LEU300 |
| C | ARG303 |
| C | MET304 |
| C | HOH627 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 403 |
| Chain | Residue |
| C | ARG115 |
| C | ARG149 |
| C | HOH617 |
| C | HOH632 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 404 |
| Chain | Residue |
| C | HIS43 |
| C | ALA46 |
| C | ARG57 |
| C | HOH517 |
| C | HOH658 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {} |
| Chain | Residue | Details |
