2WES
Crystal structures of mutant E46Q of tryptophan 5-halogenase (PyrH)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD A 650 |
| Chain | Residue |
| A | GLY9 |
| A | GLN46 |
| A | ALA47 |
| A | ASP193 |
| A | VAL195 |
| A | CYS225 |
| A | THR226 |
| A | GLY227 |
| A | ARG229 |
| A | LEU231 |
| A | LEU345 |
| A | GLY10 |
| A | PHE349 |
| A | PRO352 |
| A | GLY357 |
| A | ILE358 |
| A | ILE361 |
| A | CL700 |
| A | HOH2017 |
| A | HOH2186 |
| A | HOH2194 |
| A | HOH2195 |
| A | GLY11 |
| A | HOH2301 |
| A | HOH2302 |
| A | HOH2303 |
| A | HOH2304 |
| A | THR12 |
| A | ALA13 |
| A | SER36 |
| A | VAL39 |
| A | ARG41 |
| A | ILE42 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 700 |
| Chain | Residue |
| A | PRO352 |
| A | THR356 |
| A | GLY357 |
| A | FAD650 |
| site_id | AC3 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD B 650 |
| Chain | Residue |
| B | GLY9 |
| B | GLY10 |
| B | GLY11 |
| B | THR12 |
| B | ALA13 |
| B | SER36 |
| B | VAL39 |
| B | ARG41 |
| B | ILE42 |
| B | GLN46 |
| B | ALA47 |
| B | ASP193 |
| B | ASP194 |
| B | VAL195 |
| B | CYS225 |
| B | THR226 |
| B | GLY227 |
| B | ARG229 |
| B | LEU231 |
| B | LEU345 |
| B | PHE349 |
| B | PRO352 |
| B | GLY357 |
| B | ILE358 |
| B | ILE361 |
| B | CL700 |
| B | HOH2004 |
| B | HOH2007 |
| B | HOH2148 |
| B | HOH2234 |
| B | HOH2235 |
| B | HOH2236 |
| B | HOH2237 |
| B | HOH2238 |
| B | HOH2239 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 700 |
| Chain | Residue |
| B | PRO352 |
| B | THR356 |
| B | GLY357 |
| B | FAD650 |
| site_id | AC5 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD C 650 |
| Chain | Residue |
| C | ILE361 |
| C | CL700 |
| C | HOH2008 |
| C | HOH2118 |
| C | HOH2120 |
| C | HOH2199 |
| C | HOH2200 |
| C | HOH2201 |
| C | HOH2202 |
| C | HOH2203 |
| C | GLY9 |
| C | GLY10 |
| C | GLY11 |
| C | THR12 |
| C | ALA13 |
| C | SER36 |
| C | VAL39 |
| C | ARG41 |
| C | ILE42 |
| C | GLN46 |
| C | ALA47 |
| C | ASP193 |
| C | VAL195 |
| C | CYS225 |
| C | THR226 |
| C | GLY227 |
| C | ARG229 |
| C | LEU231 |
| C | LEU345 |
| C | PHE349 |
| C | PRO352 |
| C | GLY357 |
| C | ILE358 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL C 700 |
| Chain | Residue |
| C | PRO352 |
| C | THR356 |
| C | GLY357 |
| C | FAD650 |
| C | HOH2119 |
| site_id | AC7 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD D 650 |
| Chain | Residue |
| D | GLY9 |
| D | GLY10 |
| D | GLY11 |
| D | THR12 |
| D | ALA13 |
| D | SER36 |
| D | VAL39 |
| D | ARG41 |
| D | ILE42 |
| D | GLN46 |
| D | ALA47 |
| D | ASP193 |
| D | VAL195 |
| D | CYS225 |
| D | THR226 |
| D | GLY227 |
| D | ARG229 |
| D | GLY344 |
| D | LEU345 |
| D | PHE349 |
| D | PRO352 |
| D | GLY357 |
| D | ILE358 |
| D | ILE361 |
| D | CL700 |
| D | HOH2105 |
| D | HOH2106 |
| D | HOH2190 |
| D | HOH2191 |
| D | HOH2192 |
| D | HOH2193 |
| D | HOH2194 |
| D | HOH2195 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL D 700 |
| Chain | Residue |
| D | PRO352 |
| D | THR356 |
| D | GLY357 |
| D | FAD650 |
| D | HOH2101 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P95480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19501593","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WES","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WET","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19501593","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WET","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19501593","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WET","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WEU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for activity","evidences":[{"source":"UniProtKB","id":"P95480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
