3BXO
Crystal Structure of Streptomyces venezuelae DesVI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0032259 | biological_process | methylation |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0032259 | biological_process | methylation |
| B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE SAM A 238 |
| Chain | Residue |
| A | TYR21 |
| A | ASP89 |
| A | MET90 |
| A | ARG91 |
| A | MET105 |
| A | PHE106 |
| A | SER108 |
| A | HOH269 |
| A | HOH291 |
| A | HOH341 |
| A | HOH362 |
| A | ALA46 |
| A | HOH402 |
| A | CYS47 |
| A | HIS52 |
| A | GLU67 |
| A | LEU68 |
| A | SER69 |
| A | MET72 |
| A | GLY88 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SAM B 238 |
| Chain | Residue |
| B | TYR21 |
| B | ALA46 |
| B | HIS52 |
| B | GLU67 |
| B | LEU68 |
| B | SER69 |
| B | MET72 |
| B | GLY88 |
| B | ASP89 |
| B | MET90 |
| B | MET105 |
| B | PHE106 |
| B | SER108 |
| B | HOH300 |
| B | HOH301 |
| B | HOH321 |
| B | HOH414 |
| B | HOH498 |
| B | HOH523 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE UPP A 239 |
| Chain | Residue |
| A | TYR14 |
| A | ARG17 |
| A | PHE106 |
| A | TRP140 |
| A | TRP141 |
| A | THR145 |
| A | PHE146 |
| A | ALA147 |
| A | TRP150 |
| A | SER152 |
| A | ARG165 |
| A | SER167 |
| A | SER169 |
| A | MET178 |
| A | ILE200 |
| A | ARG229 |
| A | HOH356 |
| A | HOH413 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE UPP B 239 |
| Chain | Residue |
| B | TYR14 |
| B | ARG17 |
| B | PHE106 |
| B | TRP140 |
| B | TRP141 |
| B | THR145 |
| B | PHE146 |
| B | ALA147 |
| B | TRP150 |
| B | SER152 |
| B | ARG165 |
| B | SER167 |
| B | SER169 |
| B | MET178 |
| B | ARG229 |
| B | HOH446 |
| B | HOH478 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 240 |
| Chain | Residue |
| B | PRO81 |
| B | ARG171 |
| B | GLY173 |
| B | HOH265 |
| B | HOH308 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:18327916 |
| Chain | Residue | Details |
| A | TYR14 | |
| B | SER152 | |
| B | ARG165 | |
| B | ARG229 | |
| A | ARG17 | |
| A | THR145 | |
| A | SER152 | |
| A | ARG165 | |
| A | ARG229 | |
| B | TYR14 | |
| B | ARG17 | |
| B | THR145 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18327916, ECO:0007744|PDB:3BXO |
| Chain | Residue | Details |
| A | TYR21 | |
| B | MET105 | |
| A | ALA46 | |
| A | GLU67 | |
| A | ASP89 | |
| A | MET105 | |
| B | TYR21 | |
| B | ALA46 | |
| B | GLU67 | |
| B | ASP89 |
