Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0047651 | molecular_function | alkylhalidase activity |
| A | 0071949 | molecular_function | FAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0047651 | molecular_function | alkylhalidase activity |
| B | 0071949 | molecular_function | FAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0047651 | molecular_function | alkylhalidase activity |
| C | 0071949 | molecular_function | FAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 0047651 | molecular_function | alkylhalidase activity |
| D | 0071949 | molecular_function | FAD binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0017000 | biological_process | antibiotic biosynthetic process |
| E | 0047651 | molecular_function | alkylhalidase activity |
| E | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | binding site for residue FAD E 501 |
| Chain | Residue |
| E | GLY12 |
| E | HIS43 |
| E | VAL44 |
| E | GLY45 |
| E | SER47 |
| E | ARG123 |
| E | GLU146 |
| E | ILE147 |
| E | ALA179 |
| E | SER180 |
| E | GLY181 |
| E | GLY14 |
| E | ASN183 |
| E | ALA203 |
| E | TRP239 |
| E | ILE241 |
| E | GLY315 |
| E | ASP316 |
| E | PHE320 |
| E | PRO323 |
| E | SER326 |
| E | GLY328 |
| E | PRO15 |
| E | VAL329 |
| E | HOH602 |
| E | HOH603 |
| E | HOH605 |
| E | ALA16 |
| E | PHE34 |
| E | GLU35 |
| E | LYS36 |
| E | GLU37 |
| E | ARG41 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue CL E 502 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CL E 503 |
| Chain | Residue |
| E | PHE320 |
| E | PRO323 |
| E | SER327 |
| E | GLY328 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | GLY12 |
| A | GLY13 |
| A | PRO15 |
| A | ALA16 |
| A | GLU35 |
| A | LYS36 |
| A | GLU37 |
| A | ARG41 |
| A | HIS43 |
| A | VAL44 |
| A | GLY45 |
| A | SER47 |
| A | ARG123 |
| A | GLU146 |
| A | ILE147 |
| A | SER180 |
| A | GLY181 |
| A | ARG182 |
| A | ASN183 |
| A | LEU185 |
| A | ALA203 |
| A | ILE241 |
| A | GLY315 |
| A | ASP316 |
| A | PHE320 |
| A | PRO323 |
| A | SER326 |
| A | GLY328 |
| A | VAL329 |
| A | CL502 |
| A | HOH602 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| A | PHE320 |
| A | PRO323 |
| A | SER327 |
| A | GLY328 |
| A | FAD501 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 503 |
| Chain | Residue |
| A | ARG277 |
| A | ASN279 |
| site_id | AC7 |
| Number of Residues | 34 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | ALA203 |
| B | GLY315 |
| B | ASP316 |
| B | PHE320 |
| B | PRO323 |
| B | SER326 |
| B | GLY328 |
| B | VAL329 |
| B | ALA332 |
| B | CL503 |
| B | HOH601 |
| B | ILE11 |
| B | GLY12 |
| B | GLY14 |
| B | PRO15 |
| B | ALA16 |
| B | PHE34 |
| B | GLU35 |
| B | LYS36 |
| B | GLU37 |
| B | ARG41 |
| B | HIS43 |
| B | VAL44 |
| B | GLY45 |
| B | GLU46 |
| B | SER47 |
| B | ARG123 |
| B | GLU146 |
| B | ILE147 |
| B | ALA179 |
| B | SER180 |
| B | GLY181 |
| B | ARG182 |
| B | ASN183 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 502 |
| Chain | Residue |
| B | ARG277 |
| B | GLU278 |
| B | ASN279 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 503 |
| Chain | Residue |
| B | PRO323 |
| B | SER327 |
| B | GLY328 |
| B | FAD501 |
| site_id | AD1 |
| Number of Residues | 31 |
| Details | binding site for residue FAD C 501 |
| Chain | Residue |
| C | GLY12 |
| C | GLY14 |
| C | PRO15 |
| C | ALA16 |
| C | PHE34 |
| C | GLU35 |
| C | LYS36 |
| C | GLU37 |
| C | ARG41 |
| C | HIS43 |
| C | VAL44 |
| C | GLY45 |
| C | GLU46 |
| C | SER47 |
| C | ARG123 |
| C | ILE147 |
| C | ALA179 |
| C | SER180 |
| C | GLY181 |
| C | ASN183 |
| C | ALA203 |
| C | TRP239 |
| C | ILE241 |
| C | GLY315 |
| C | ASP316 |
| C | PHE320 |
| C | PRO323 |
| C | SER326 |
| C | GLY328 |
| C | VAL329 |
| C | CL503 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue CL C 502 |
| Chain | Residue |
| C | ARG277 |
| C | ASN279 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue CL C 503 |
| Chain | Residue |
| C | PHE320 |
| C | PRO323 |
| C | SER327 |
| C | GLY328 |
| C | FAD501 |
| site_id | AD4 |
| Number of Residues | 30 |
| Details | binding site for residue FAD D 501 |
| Chain | Residue |
| D | ILE11 |
| D | GLY12 |
| D | GLY14 |
| D | PRO15 |
| D | ALA16 |
| D | PHE34 |
| D | GLU35 |
| D | LYS36 |
| D | GLU37 |
| D | ARG41 |
| D | HIS43 |
| D | VAL44 |
| D | GLY45 |
| D | GLU46 |
| D | SER47 |
| D | ARG123 |
| D | ILE147 |
| D | ALA179 |
| D | SER180 |
| D | GLY181 |
| D | ASN183 |
| D | ALA203 |
| D | ILE241 |
| D | GLY315 |
| D | ASP316 |
| D | PHE320 |
| D | PRO323 |
| D | SER326 |
| D | GLY328 |
| D | VAL329 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue CL D 502 |
| Chain | Residue |
| D | ARG277 |
| D | ASN279 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 50 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26416533","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DBJ","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26416533","evidenceCode":"ECO:0000269"}]} |