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 | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 B 290 |
| Chain | Residue |
| A | CYS94 |
| A | CYS129 |
| A | GLY131 |
| B | CYS94 |
| B | ALA95 |
| B | CYS129 |
| B | GLY131 |
| B | HOH346 |
| site_id | FES |
| Number of Residues | 4 |
| Details | THE FS4 IS COVALENTLY BONDED THROUGH ITS FE ATOMS TO THE GAMMA SULFURS OF CYS 94 AND CYS 129 OF EACH SUBUNIT. |
| Chain | Residue |
| A | CYS94 |
| A | CYS129 |
| B | CYS94 |
| B | CYS129 |
| site_id | WMA |
| Number of Residues | 16 |
| Details | WALKER A MOTIF |
| Chain | Residue |
| A | GLY13 |
| A | LYS14 |
| A | SER15 |
| B | GLY8 |
| B | LYS9 |
| B | GLY10 |
| B | GLY11 |
| B | ILE12 |
| B | GLY13 |
| B | LYS14 |
| B | SER15 |
| A | GLY8 |
| A | LYS9 |
| A | GLY10 |
| A | GLY11 |
| A | ILE12 |
| site_id | WMB |
| Number of Residues | 2 |
| Details | WALKER B MOTIF |
| Chain | Residue |
| A | ASP122 |
| B | ASP122 |
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 | ASP122-PRO135 | |
| site_id | PS00746 |
| Number of Residues | 13 |
| Details | NIFH_FRXC_1 NifH/frxC family signature 1. EsGGPepGvGCAG |
| Chain | Residue | Details |
| A | GLU84-GLY96 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY8 | |
| B | GLY8 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | CYS94 | |
| A | CYS129 | |
| B | CYS94 | |
| B | CYS129 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG97 | |
| B | ARG97 | |
