Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0051539 | molecular_function | 4 iron, 4 sulfur cluster 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 | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 291 |
| Chain | Residue |
| A | GLY14 |
| A | SER16 |
| A | HOH5011 |
| A | HOH5013 |
| B | ADP292 |
| B | HOH5012 |
| B | HOH5014 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 291 |
| Chain | Residue |
| B | GLY14 |
| B | SER16 |
| B | HOH5025 |
| B | HOH5026 |
| B | HOH5027 |
| B | HOH5028 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 B 290 |
| Chain | Residue |
| A | CYS97 |
| A | ALA98 |
| A | CYS132 |
| A | GLY133 |
| A | GLY134 |
| B | CYS97 |
| B | ALA98 |
| B | CYS132 |
| B | GLY134 |
| B | PHE135 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADP B 292 |
| Chain | Residue |
| A | GLY11 |
| A | GLY12 |
| A | ILE13 |
| A | LYS41 |
| A | ALA42 |
| A | MG291 |
| A | HOH5013 |
| B | LYS10 |
| B | GLY11 |
| B | GLY128 |
| B | ASP129 |
| B | MET156 |
| B | ALA160 |
| B | HOH298 |
| B | HOH5012 |
| B | HOH5014 |
| site_id | ATP |
| Number of Residues | 4 |
| Details | A POSSIBLE SITE FOR ATP HYDROLYSIS |
| Chain | Residue |
| A | ASP39 |
| A | ASP43 |
| B | ASP39 |
| B | ASP43 |
| site_id | FES |
| Number of Residues | 4 |
| Details | THE 4S-FE CLUSTER |
| Chain | Residue |
| A | CYS97 |
| A | CYS132 |
| B | CYS97 |
| B | CYS132 |
| site_id | WMA |
| Number of Residues | 16 |
| Details | WALKER A MOTIF |
| Chain | Residue |
| A | GLY14 |
| A | LYS15 |
| A | SER16 |
| B | GLY9 |
| B | LYS10 |
| B | GLY11 |
| B | GLY12 |
| B | ILE13 |
| B | GLY14 |
| B | LYS15 |
| B | SER16 |
| A | GLY9 |
| A | LYS10 |
| A | GLY11 |
| A | GLY12 |
| A | ILE13 |
| site_id | WMB |
| Number of Residues | 2 |
| Details | WALKER B MOTIF |
| Chain | Residue |
| A | ASP125 |
| B | ASP125 |
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 | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS10 | |
| A | ALA98 | |
| A | GLY133 | |
| B | LYS10 | |
| B | ALA98 | |
| B | GLY133 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY101 | |
| B | GLY101 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1f48 |
| Chain | Residue | Details |
| A | LYS15 | |
| A | GLY12 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1f48 |
| Chain | Residue | Details |
| B | LYS15 | |
| B | GLY12 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 212 |
| Chain | Residue | Details |
| A | GLY11 | electrostatic stabiliser, hydrogen bond donor |
| A | SER16 | electrostatic stabiliser, hydrogen bond donor |
| A | ALA42 | electrostatic stabiliser, hydrogen bond donor |
| A | VAL130 | 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 | GLY11 | electrostatic stabiliser, hydrogen bond donor |
| B | SER16 | electrostatic stabiliser, hydrogen bond donor |
| B | ALA42 | electrostatic stabiliser, hydrogen bond donor |
| B | VAL130 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
