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 | 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 | 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: |
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 |