Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016853 | molecular_function | isomerase activity |
A | 0017000 | biological_process | antibiotic biosynthetic process |
B | 0016853 | molecular_function | isomerase activity |
B | 0017000 | biological_process | antibiotic biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE LSD A 301 |
Chain | Residue |
A | ASP170 |
A | TRP270 |
A | HOH437 |
B | HIS232 |
B | HOH452 |
A | SER174 |
A | TRP175 |
A | TRP175 |
A | ARG177 |
A | HIS186 |
A | SER224 |
A | HIS231 |
A | TYR251 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 302 |
Chain | Residue |
A | HIS146 |
A | ASP170 |
A | GLU197 |
A | TYR251 |
A | MET253 |
A | MET266 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT A 303 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT A 304 |
Chain | Residue |
A | TYR14 |
A | ASP38 |
A | GLU65 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE FMT A 305 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 306 |
Chain | Residue |
A | VAL123 |
A | SER126 |
A | THR129 |
A | HOH449 |
A | HOH451 |
site_id | AC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE LSD B 301 |
Chain | Residue |
A | HIS232 |
B | ASP170 |
B | SER174 |
B | TRP175 |
B | TRP175 |
B | ARG177 |
B | HIS186 |
B | SER224 |
B | LEU228 |
B | HIS231 |
B | LEU233 |
B | TYR251 |
B | HOH422 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 302 |
Chain | Residue |
B | HIS146 |
B | ASP170 |
B | GLU197 |
B | TYR251 |
B | MET253 |
B | MET266 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT B 303 |
Chain | Residue |
B | THR198 |
B | GLY200 |
B | THR214 |
B | SER216 |
B | HOH423 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT B 304 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT B 305 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT B 306 |
Chain | Residue |
A | HIS74 |
B | HIS232 |
B | ALA272 |
B | NA308 |
B | HOH420 |
B | HOH429 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT B 307 |
Chain | Residue |
A | HIS232 |
B | HIS74 |
B | NA308 |
B | HOH419 |
B | HOH439 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA B 308 |
Chain | Residue |
A | HIS232 |
B | HIS232 |
B | FMT306 |
B | FMT307 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 309 |
Chain | Residue |
B | VAL123 |
B | SER126 |
B | THR129 |
B | HOH465 |
B | HOH466 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor; for 5-exo epoxide-opening cyclization activity => ECO:0000269|PubMed:22388816 |
Chain | Residue | Details |
A | ASP38 | |
B | ASP38 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor; for 6-endo epoxide-opening cyclization activity => ECO:0000269|PubMed:22388816 |
Chain | Residue | Details |
A | ASP170 | |
B | ASP170 | |
Chain | Residue | Details |
A | TYR14 | |
B | ARG177 | |
B | GLU197 | |
B | TYR251 | |
A | GLU65 | |
A | HIS146 | |
A | ARG177 | |
A | GLU197 | |
A | TYR251 | |
B | TYR14 | |
B | GLU65 | |
B | HIS146 | |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Raises pKa of active site Asp-38 |
Chain | Residue | Details |
A | ARG54 | |
B | ARG54 | |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Raises pKa of active site Asp-170 |
Chain | Residue | Details |
A | HIS186 | |
B | HIS186 | |