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 | 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 | 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 | 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 |