5EEH
Crystal structure of carminomycin-4-O-methyltransferase DnrK in complex with SAH and 2-chloro-4-nitrophenol
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008171 | molecular_function | O-methyltransferase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0032259 | biological_process | methylation |
| A | 1901771 | biological_process | daunorubicin biosynthetic process |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008171 | molecular_function | O-methyltransferase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0032259 | biological_process | methylation |
| B | 1901771 | biological_process | daunorubicin biosynthetic process |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0008171 | molecular_function | O-methyltransferase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0032259 | biological_process | methylation |
| C | 1901771 | biological_process | daunorubicin biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue SAH A 401 |
| Chain | Residue |
| A | TYR143 |
| A | SER252 |
| A | PHE253 |
| A | ASN257 |
| A | P9P404 |
| A | HOH534 |
| A | HOH535 |
| A | HOH638 |
| A | HOH662 |
| A | HOH677 |
| A | ARG153 |
| A | LEU160 |
| A | GLY187 |
| A | GLU210 |
| A | MET211 |
| A | GLY236 |
| A | ASP237 |
| A | PHE238 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue P9P A 402 |
| Chain | Residue |
| A | TRP106 |
| A | VAL113 |
| A | PHE142 |
| A | PHE156 |
| A | LEU160 |
| A | ASN257 |
| A | ARG303 |
| A | MET304 |
| A | PHE307 |
| A | LEU308 |
| A | P9P403 |
| A | P9P404 |
| A | HOH504 |
| A | HOH635 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue P9P A 403 |
| Chain | Residue |
| A | TRP106 |
| A | ASP163 |
| A | TYR342 |
| A | P9P402 |
| A | P9P404 |
| A | P9P405 |
| A | HOH588 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue P9P A 404 |
| Chain | Residue |
| A | LEU160 |
| A | VAL166 |
| A | ALA167 |
| A | PHE253 |
| A | LEU300 |
| A | SAH401 |
| A | P9P402 |
| A | P9P403 |
| A | HOH667 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue P9P A 405 |
| Chain | Residue |
| A | ILE21 |
| A | ALA101 |
| A | GLN103 |
| A | ASP163 |
| A | THR339 |
| A | ILE340 |
| A | P9P403 |
| A | P9P406 |
| A | SO4409 |
| B | P9P401 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue P9P A 406 |
| Chain | Residue |
| A | ARG18 |
| A | ILE21 |
| A | GLU295 |
| A | GLN296 |
| A | GLU299 |
| A | ILE340 |
| A | P9P405 |
| A | SO4409 |
| A | HOH514 |
| A | HOH551 |
| A | HOH653 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue P9P A 407 |
| Chain | Residue |
| A | ALA173 |
| A | ARG200 |
| A | HOH625 |
| B | LEU94 |
| B | HIS99 |
| B | P9P406 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 408 |
| Chain | Residue |
| A | ARG61 |
| A | ARG131 |
| A | HIS261 |
| A | HOH516 |
| A | HOH606 |
| A | HOH612 |
| A | HOH687 |
| A | HOH697 |
| B | ARG128 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 409 |
| Chain | Residue |
| A | GLN103 |
| A | TRP106 |
| A | ARG303 |
| A | P9P405 |
| A | P9P406 |
| A | HOH670 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 410 |
| Chain | Residue |
| A | ARG115 |
| A | ARG149 |
| A | HOH502 |
| A | HOH521 |
| B | ARG265 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 411 |
| Chain | Residue |
| A | HIS43 |
| A | ALA46 |
| A | HOH501 |
| A | HOH518 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue P9P B 401 |
| Chain | Residue |
| A | GLN13 |
| A | ILE14 |
| A | LEU17 |
| A | HIS99 |
| A | P9P405 |
| B | ARG200 |
| B | HOH638 |
| site_id | AD4 |
| Number of Residues | 21 |
| Details | binding site for residue SAH B 402 |
| 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 | TRP258 |
| B | P9P405 |
| B | HOH513 |
| B | HOH596 |
| B | HOH607 |
| B | HOH613 |
| B | HOH634 |
| B | HOH643 |
| B | HOH650 |
| site_id | AD5 |
| Number of Residues | 14 |
| Details | binding site for residue P9P B 403 |
| Chain | Residue |
| B | TRP106 |
| B | VAL113 |
| B | PHE142 |
| B | PHE156 |
| B | LEU160 |
| B | ASN257 |
| B | ARG303 |
| B | MET304 |
| B | PHE307 |
| B | LEU308 |
| B | P9P404 |
| B | P9P405 |
| B | HOH504 |
| B | HOH602 |
| site_id | AD6 |
| Number of Residues | 9 |
| Details | binding site for residue P9P B 404 |
| Chain | Residue |
| B | TRP106 |
| B | ASP163 |
| B | TYR342 |
| B | P9P403 |
| B | P9P405 |
| B | P9P406 |
| B | P9P407 |
| B | HOH587 |
| B | HOH608 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for residue P9P B 405 |
| Chain | Residue |
| B | LEU160 |
| B | ALA167 |
| B | PHE253 |
| B | LEU300 |
| B | SAH402 |
| B | P9P403 |
| B | P9P404 |
| site_id | AD8 |
| Number of Residues | 9 |
| Details | binding site for residue P9P B 406 |
| Chain | Residue |
| A | P9P407 |
| B | ALA101 |
| B | GLN103 |
| B | ASP163 |
| B | THR339 |
| B | ILE340 |
| B | P9P404 |
| B | P9P407 |
| B | SO4409 |
| site_id | AD9 |
| Number of Residues | 8 |
| Details | binding site for residue P9P B 407 |
| Chain | Residue |
| B | GLU295 |
| B | GLU299 |
| B | ILE340 |
| B | P9P404 |
| B | P9P406 |
| B | SO4409 |
| B | HOH510 |
| B | HOH608 |
| site_id | AE1 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 408 |
| Chain | Residue |
| B | ARG131 |
| B | PRO259 |
| B | HIS261 |
| B | HOH509 |
| B | HOH522 |
| B | HOH597 |
| B | HOH656 |
| B | HOH672 |
| site_id | AE2 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 409 |
| Chain | Residue |
| B | GLN103 |
| B | TRP106 |
| B | ARG303 |
| B | P9P406 |
| B | P9P407 |
| B | HOH519 |
| B | HOH683 |
| site_id | AE3 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 410 |
| Chain | Residue |
| B | ARG115 |
| B | ARG149 |
| site_id | AE4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 411 |
| Chain | Residue |
| B | ARG61 |
| B | PRO62 |
| B | GLU63 |
| site_id | AE5 |
| Number of Residues | 17 |
| Details | binding site for residue SAH C 401 |
| Chain | Residue |
| C | TYR143 |
| C | ARG153 |
| C | LEU160 |
| C | PHE168 |
| C | GLY187 |
| C | GLY189 |
| C | GLU210 |
| C | MET211 |
| C | GLY236 |
| C | ASP237 |
| C | PHE238 |
| C | SER252 |
| C | PHE253 |
| C | ASN257 |
| C | P9P403 |
| C | HOH594 |
| C | HOH614 |
| site_id | AE6 |
| Number of Residues | 13 |
| Details | binding site for residue P9P C 402 |
| Chain | Residue |
| C | TRP106 |
| C | VAL113 |
| C | PHE142 |
| C | PHE156 |
| C | ASN257 |
| C | ARG303 |
| C | MET304 |
| C | PHE307 |
| C | LEU308 |
| C | P9P403 |
| C | P9P404 |
| C | HOH502 |
| C | HOH616 |
| site_id | AE7 |
| Number of Residues | 8 |
| Details | binding site for residue P9P C 403 |
| Chain | Residue |
| C | LEU160 |
| C | PHE168 |
| C | PHE253 |
| C | LEU300 |
| C | SAH401 |
| C | P9P402 |
| C | P9P404 |
| C | HOH646 |
| site_id | AE8 |
| Number of Residues | 5 |
| Details | binding site for residue P9P C 404 |
| Chain | Residue |
| C | TYR342 |
| C | P9P402 |
| C | P9P403 |
| C | HOH616 |
| C | HOH646 |
| site_id | AE9 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 C 405 |
| Chain | Residue |
| C | ARG115 |
| C | ARG149 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | ASP163 | |
| B | GLY187 | |
| B | GLU210 | |
| B | ASP237 | |
| B | SER252 | |
| B | ASN257 | |
| B | ARG303 | |
| C | ARG153 | |
| C | ASP163 | |
| C | GLY187 | |
| C | GLU210 | |
| C | ASP237 | |
| C | SER252 | |
| C | ASN257 | |
| C | ARG303 | |
| A | ARG153 | |
| A | ASP163 | |
| A | GLY187 | |
| A | GLU210 | |
| A | ASP237 | |
| A | SER252 | |
| A | ASN257 | |
| A | ARG303 | |
| B | ARG153 |
