6NIE
BesD with Fe(II), chloride, and alpha-ketoglutarate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0062142 | biological_process | L-beta-ethynylserine biosynthetic process |
| A | 0062143 | biological_process | L-propargylglycine biosynthetic process |
| A | 0062147 | molecular_function | L-lysine 4-chlorinase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0062142 | biological_process | L-beta-ethynylserine biosynthetic process |
| B | 0062143 | biological_process | L-propargylglycine biosynthetic process |
| B | 0062147 | molecular_function | L-lysine 4-chlorinase activity |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0062142 | biological_process | L-beta-ethynylserine biosynthetic process |
| C | 0062143 | biological_process | L-propargylglycine biosynthetic process |
| C | 0062147 | molecular_function | L-lysine 4-chlorinase activity |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 0062142 | biological_process | L-beta-ethynylserine biosynthetic process |
| D | 0062143 | biological_process | L-propargylglycine biosynthetic process |
| D | 0062147 | molecular_function | L-lysine 4-chlorinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue LYS A 301 |
| Chain | Residue |
| A | ARG74 |
| A | HOH487 |
| A | HOH521 |
| A | HOH522 |
| A | GLU120 |
| A | HIS134 |
| A | HIS137 |
| A | TRP138 |
| A | THR221 |
| A | TRP238 |
| A | TRP239 |
| A | HOH434 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue FE2 A 302 |
| Chain | Residue |
| A | HIS137 |
| A | HIS204 |
| A | CL303 |
| A | AKG304 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 303 |
| Chain | Residue |
| A | HIS137 |
| A | TRP138 |
| A | GLY139 |
| A | HIS204 |
| A | FE2302 |
| A | AKG304 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue AKG A 304 |
| Chain | Residue |
| A | HIS134 |
| A | HIS137 |
| A | TYR195 |
| A | HIS204 |
| A | THR206 |
| A | ARG215 |
| A | ASN219 |
| A | FE2302 |
| A | CL303 |
| A | HOH491 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue LYS B 301 |
| Chain | Residue |
| B | ARG74 |
| B | GLU120 |
| B | HIS134 |
| B | HIS137 |
| B | TRP138 |
| B | ASN219 |
| B | THR221 |
| B | TRP238 |
| B | TRP239 |
| B | HOH416 |
| B | HOH487 |
| B | HOH488 |
| B | HOH491 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue FE2 B 302 |
| Chain | Residue |
| B | HIS137 |
| B | HIS204 |
| B | CL303 |
| B | AKG304 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue CL B 303 |
| Chain | Residue |
| B | HIS137 |
| B | TRP138 |
| B | GLY139 |
| B | THR199 |
| B | HIS204 |
| B | FE2302 |
| B | AKG304 |
| B | HOH491 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue AKG B 304 |
| Chain | Residue |
| B | HIS134 |
| B | HIS137 |
| B | TYR195 |
| B | HIS204 |
| B | THR206 |
| B | ARG215 |
| B | ASN219 |
| B | FE2302 |
| B | CL303 |
| B | HOH419 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue FE B 305 |
| Chain | Residue |
| A | HIS113 |
| A | GLU225 |
| B | GLU225 |
| B | HOH412 |
| B | HOH464 |
| D | HOH410 |
| site_id | AD1 |
| Number of Residues | 11 |
| Details | binding site for residue LYS C 301 |
| Chain | Residue |
| C | ARG74 |
| C | GLU120 |
| C | HIS134 |
| C | HIS137 |
| C | TRP138 |
| C | ASN219 |
| C | THR221 |
| C | TRP238 |
| C | HOH417 |
| C | HOH467 |
| C | HOH480 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue FE2 C 302 |
| Chain | Residue |
| C | HIS137 |
| C | HIS204 |
| C | CL303 |
| C | AKG304 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue CL C 303 |
| Chain | Residue |
| C | HIS137 |
| C | TRP138 |
| C | GLY139 |
| C | HIS204 |
| C | FE2302 |
| C | AKG304 |
| site_id | AD4 |
| Number of Residues | 11 |
| Details | binding site for residue AKG C 304 |
| Chain | Residue |
| C | ARG215 |
| C | ILE217 |
| C | ASN219 |
| C | FE2302 |
| C | CL303 |
| C | HOH474 |
| C | HIS134 |
| C | HIS137 |
| C | TYR195 |
| C | HIS204 |
| C | THR206 |
| site_id | AD5 |
| Number of Residues | 12 |
| Details | binding site for residue LYS D 301 |
| Chain | Residue |
| D | ARG74 |
| D | GLU120 |
| D | HIS134 |
| D | HIS137 |
| D | TRP138 |
| D | ASN219 |
| D | THR221 |
| D | TRP238 |
| D | TRP239 |
| D | HOH432 |
| D | HOH473 |
| D | HOH494 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue FE2 D 302 |
| Chain | Residue |
| D | HIS137 |
| D | HIS204 |
| D | CL303 |
| D | AKG304 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue CL D 303 |
| Chain | Residue |
| D | HIS137 |
| D | GLY139 |
| D | HIS204 |
| D | FE2302 |
| D | AKG304 |
| site_id | AD8 |
| Number of Residues | 12 |
| Details | binding site for residue AKG D 304 |
| Chain | Residue |
| D | HIS134 |
| D | HIS137 |
| D | ILE146 |
| D | TYR195 |
| D | HIS204 |
| D | THR206 |
| D | ARG215 |
| D | ILE217 |
| D | ASN219 |
| D | FE2302 |
| D | CL303 |
| D | HOH451 |
