Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008860 | molecular_function | ferredoxin-NAD+ reductase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042203 | biological_process | toluene catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue FES A 401 |
| Chain | Residue |
| A | TYR34 |
| A | CYS76 |
| A | GLU35 |
| A | CYS36 |
| A | ASN37 |
| A | GLY39 |
| A | GLY40 |
| A | CYS41 |
| A | GLY42 |
| A | CYS44 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | binding site for residue FAD A 402 |
| Chain | Residue |
| A | CYS36 |
| A | SER38 |
| A | TRP57 |
| A | TYR135 |
| A | ARG146 |
| A | ALA147 |
| A | TYR148 |
| A | SER149 |
| A | ILE162 |
| A | VAL163 |
| A | LYS164 |
| A | GLY169 |
| A | LYS170 |
| A | VAL171 |
| A | SER172 |
| A | SER209 |
| A | ALA212 |
| A | PHE325 |
| A | HOH667 |
| A | HOH668 |
| A | HOH697 |
| A | HOH710 |
| A | HOH747 |
| A | HOH763 |
| A | HOH787 |
| A | HOH907 |
| A | HOH912 |
| A | HOH914 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue NI A 403 |
| Chain | Residue |
| A | HIS12 |
| A | BTB407 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue NI A 404 |
| Chain | Residue |
| A | HIS11 |
| A | GLU29 |
| A | HOH644 |
| A | HOH657 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue NI A 405 |
| Chain | Residue |
| A | HIS278 |
| A | BTB408 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue BTB A 406 |
| Chain | Residue |
| A | SER97 |
| A | HIS98 |
| A | PHE130 |
| A | SER131 |
| A | VAL140 |
| A | PRO141 |
| A | GLU142 |
| A | GLU178 |
| A | NI409 |
| A | HOH511 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue BTB A 407 |
| Chain | Residue |
| A | HIS12 |
| A | ASP115 |
| A | NI403 |
| A | HOH507 |
| A | HOH509 |
| A | HOH528 |
| A | HOH564 |
| A | HOH590 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue BTB A 408 |
| Chain | Residue |
| A | PRO61 |
| A | GLY62 |
| A | LEU63 |
| A | ALA64 |
| A | HIS278 |
| A | GLU279 |
| A | NI405 |
| A | HOH501 |
| A | HOH517 |
| A | HOH539 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue NI A 409 |
| Chain | Residue |
| A | HIS98 |
| A | GLU178 |
| A | BTB406 |
Functional Information from PROSITE/UniProt
| site_id | PS00197 |
| Number of Residues | 9 |
| Details | 2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CNSGGCGAC |
| Chain | Residue | Details |
| A | CYS36-CYS44 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 95 |
| Details | Domain: {"description":"FAD-binding FR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00716","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 231 |
| Details | Region: {"description":"Ferredoxin-reductase"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26309236","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WQM","evidenceCode":"ECO:0007744"}]} |
