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 |