Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030152 | biological_process | bacteriocin biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue SAM A 501 |
| Chain | Residue |
| A | PHE123 |
| A | SER211 |
| A | ARG223 |
| A | THR251 |
| A | LYS279 |
| A | THR280 |
| A | LEU281 |
| A | ALA286 |
| A | SF4502 |
| A | HOH655 |
| A | HOH852 |
| A | CYS124 |
| A | TYR125 |
| A | THR159 |
| A | GLY161 |
| A | GLU162 |
| A | PHE186 |
| A | SER187 |
| A | ASN188 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 A 502 |
| Chain | Residue |
| A | CYS117 |
| A | CYS121 |
| A | CYS124 |
| A | SER128 |
| A | GLY161 |
| A | ASN188 |
| A | ARG223 |
| A | ARG285 |
| A | SAM501 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue FES A 503 |
| Chain | Residue |
| A | PRO335 |
| A | CYS351 |
| A | CYS385 |
| A | LYS386 |
| A | CYS387 |
| A | HOH990 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue MG A 504 |
| Chain | Residue |
| A | HOH684 |
| A | HOH684 |
| A | HOH765 |
| A | HOH765 |
| A | HOH939 |
| A | HOH939 |
| A | HOH957 |
| A | HOH957 |
Functional Information from PROSITE/UniProt
| site_id | PS01305 |
| Number of Residues | 12 |
| Details | MOAA_NIFB_PQQE moaA / nifB / pqqE family signature. LtnaCNLSCsFC |
| Chain | Residue | Details |
| A | LEU113-CYS124 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | CYS117 | |
| A | CYS121 | |
| A | CYS124 | |
| A | CYS380 | |
| A | CYS385 | |
| A | CYS387 | |
