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 |
A | ARG153 | |
B | ASP163 | |
B | GLY187 | |
B | GLU210 | |
B | ASP237 | |
B | SER252 | |
B | ASN257 | |
B | ARG303 | |
C | ARG153 | |
C | ASP163 | |
C | GLY187 | |
A | ASP163 | |
C | GLU210 | |
C | ASP237 | |
C | SER252 | |
C | ASN257 | |
C | ARG303 | |
A | GLY187 | |
A | GLU210 | |
A | ASP237 | |
A | SER252 | |
A | ASN257 | |
A | ARG303 | |
B | ARG153 |