Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0009399 | biological_process | nitrogen fixation |
| A | 0016163 | molecular_function | nitrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0009399 | biological_process | nitrogen fixation |
| B | 0016163 | molecular_function | nitrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 293 |
| Chain | Residue |
| A | LYS15 |
| A | SER16 |
| A | ASP43 |
| A | SER44 |
| A | ADP291 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 294 |
| Chain | Residue |
| B | SER16 |
| B | ASP43 |
| B | ADP292 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 A 290 |
| Chain | Residue |
| A | ALA98 |
| A | CYS132 |
| A | GLY134 |
| B | CYS97 |
| B | ALA98 |
| B | CYS132 |
| B | GLY134 |
| B | PHE135 |
| A | CYS97 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADP A 291 |
| Chain | Residue |
| A | LYS10 |
| A | GLY11 |
| A | GLY12 |
| A | ILE13 |
| A | GLY14 |
| A | LYS15 |
| A | SER16 |
| A | THR17 |
| A | ASN185 |
| A | PRO212 |
| A | ARG213 |
| A | ASP214 |
| A | VAL217 |
| A | GLN218 |
| A | GLU221 |
| A | MG293 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADP B 292 |
| Chain | Residue |
| B | LYS10 |
| B | GLY12 |
| B | ILE13 |
| B | GLY14 |
| B | LYS15 |
| B | SER16 |
| B | THR17 |
| B | ASN185 |
| B | VAL211 |
| B | PRO212 |
| B | ARG213 |
| B | ASP214 |
| B | VAL217 |
| B | GLU221 |
| B | TYR240 |
| B | MG294 |
Functional Information from PROSITE/UniProt
| site_id | PS00692 |
| Number of Residues | 14 |
| Details | NIFH_FRXC_2 NifH/frxC family signature 2. DvLGDVVCGGFAmP |
| Chain | Residue | Details |
| A | ASP125-PRO138 | |
| site_id | PS00746 |
| Number of Residues | 13 |
| Details | NIFH_FRXC_1 NifH/frxC family signature 1. EsGGPepGvGCAG |
| Chain | Residue | Details |
| A | GLU87-GLY99 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 212 |
| Chain | Residue | Details |
| A | LYS10 | electrostatic stabiliser, hydrogen bond donor |
| A | LYS15 | electrostatic stabiliser, hydrogen bond donor |
| A | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP129 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 212 |
| Chain | Residue | Details |
| B | LYS10 | electrostatic stabiliser, hydrogen bond donor |
| B | LYS15 | electrostatic stabiliser, hydrogen bond donor |
| B | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP129 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
