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 | |