1N2C
NITROGENASE COMPLEX FROM AZOTOBACTER VINELANDII STABILIZED BY ADP-TETRAFLUOROALUMINATE
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 | 0016612 | cellular_component | molybdenum-iron nitrogenase complex |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-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 | 0016612 | cellular_component | molybdenum-iron nitrogenase complex |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0009399 | biological_process | nitrogen fixation |
| C | 0016163 | molecular_function | nitrogenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016612 | cellular_component | molybdenum-iron nitrogenase complex |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0009399 | biological_process | nitrogen fixation |
| D | 0016163 | molecular_function | nitrogenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016612 | cellular_component | molybdenum-iron nitrogenase complex |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0009399 | biological_process | nitrogen fixation |
| E | 0016163 | molecular_function | nitrogenase activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0009399 | biological_process | nitrogen fixation |
| F | 0016163 | molecular_function | nitrogenase activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| G | 0005524 | molecular_function | ATP binding |
| G | 0009399 | biological_process | nitrogen fixation |
| G | 0016163 | molecular_function | nitrogenase activity |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| H | 0005524 | molecular_function | ATP binding |
| H | 0009399 | biological_process | nitrogen fixation |
| H | 0016163 | molecular_function | nitrogenase activity |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0046872 | molecular_function | metal ion binding |
| H | 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 CA D 524 |
| Chain | Residue |
| A | LYS433 |
| B | ARG108 |
| B | GLU109 |
| D | ASP353 |
| D | ASP357 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 524 |
| Chain | Residue |
| D | GLU109 |
| B | ASP353 |
| B | ASP357 |
| C | LYS433 |
| D | ARG108 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 292 |
| Chain | Residue |
| E | SER16 |
| E | ASP39 |
| E | ADP291 |
| E | ALF293 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ALF E 293 |
| Chain | Residue |
| E | GLY11 |
| E | GLY12 |
| E | LYS15 |
| E | SER16 |
| E | ASP39 |
| E | LYS41 |
| E | ASP43 |
| E | GLY128 |
| E | ADP291 |
| E | MG292 |
| F | LYS10 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG F 292 |
| Chain | Residue |
| F | SER16 |
| F | ASP39 |
| F | ASP43 |
| F | ADP291 |
| F | ALF293 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ALF F 293 |
| Chain | Residue |
| E | LYS10 |
| F | GLY11 |
| F | GLY12 |
| F | LYS15 |
| F | SER16 |
| F | ASP39 |
| F | LYS41 |
| F | ASP43 |
| F | GLY128 |
| F | ADP291 |
| F | MG292 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG G 292 |
| Chain | Residue |
| G | SER16 |
| G | ASP39 |
| G | ADP291 |
| G | ALF293 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ALF G 293 |
| Chain | Residue |
| G | GLY11 |
| G | GLY12 |
| G | LYS15 |
| G | SER16 |
| G | ASP39 |
| G | LYS41 |
| G | ASP43 |
| G | GLY128 |
| G | ADP291 |
| G | MG292 |
| H | LYS10 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG H 292 |
| Chain | Residue |
| H | SER16 |
| H | ASP39 |
| H | ADP291 |
| H | ALF293 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ALF H 293 |
| Chain | Residue |
| G | LYS10 |
| H | GLY11 |
| H | GLY12 |
| H | LYS15 |
| H | SER16 |
| H | ASP39 |
| H | LYS41 |
| H | ASP43 |
| H | GLY128 |
| H | ADP291 |
| H | MG292 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HCA A 494 |
| Chain | Residue |
| A | GLN191 |
| A | GLY424 |
| A | ILE425 |
| A | HIS442 |
| A | CFM496 |
| site_id | BC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CFM A 496 |
| Chain | Residue |
| A | VAL70 |
| A | ARG96 |
| A | HIS195 |
| A | TYR229 |
| A | ILE231 |
| A | CYS275 |
| A | SER278 |
| A | ILE355 |
| A | GLY356 |
| A | GLY357 |
| A | LEU358 |
| A | ARG359 |
| A | PHE381 |
| A | HIS442 |
| A | HCA494 |
| site_id | BC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CLF B 525 |
| Chain | Residue |
| B | CYS70 |
| B | PRO72 |
| B | SER92 |
| B | GLY94 |
| B | CYS95 |
| B | TYR98 |
| B | CYS153 |
| B | SER188 |
| A | CYS62 |
| A | TYR64 |
| A | PRO85 |
| A | VAL86 |
| A | CYS88 |
| A | TYR91 |
| A | CYS154 |
| A | GLY185 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HCA C 494 |
| Chain | Residue |
| C | GLN191 |
| C | GLY424 |
| C | ILE425 |
| C | HIS442 |
| C | CFM496 |
| site_id | BC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CFM C 496 |
| Chain | Residue |
| C | VAL70 |
| C | ARG96 |
| C | HIS195 |
| C | TYR229 |
| C | ILE231 |
| C | CYS275 |
| C | SER278 |
| C | ILE355 |
| C | GLY356 |
| C | GLY357 |
| C | LEU358 |
| C | ARG359 |
| C | PHE381 |
| C | HIS442 |
| C | HCA494 |
| site_id | BC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CLF D 525 |
| Chain | Residue |
| C | CYS62 |
| C | TYR64 |
| C | PRO85 |
| C | VAL86 |
| C | CYS88 |
| C | TYR91 |
| C | CYS154 |
| C | GLY185 |
| D | CYS70 |
| D | PRO72 |
| D | SER92 |
| D | GLY94 |
| D | CYS95 |
| D | TYR98 |
| D | CYS153 |
| D | SER188 |
| site_id | BC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SF4 F 290 |
| Chain | Residue |
| A | LEU158 |
| B | VAL157 |
| E | CYS97 |
| E | ALA98 |
| E | GLY99 |
| E | VAL131 |
| E | CYS132 |
| F | CYS97 |
| F | ALA98 |
| F | GLY99 |
| F | VAL131 |
| F | CYS132 |
| site_id | BC9 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADP E 291 |
| Chain | Residue |
| E | GLY12 |
| E | ILE13 |
| E | GLY14 |
| E | LYS15 |
| E | SER16 |
| E | THR17 |
| E | ASN185 |
| E | PRO212 |
| E | ARG213 |
| E | ASP214 |
| E | GLN218 |
| E | GLU221 |
| E | MG292 |
| E | ALF293 |
| F | LYS10 |
| F | GLU154 |
| F | MET156 |
| site_id | CC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADP F 291 |
| Chain | Residue |
| E | LYS10 |
| E | GLU154 |
| E | MET156 |
| F | GLY12 |
| F | ILE13 |
| F | GLY14 |
| F | LYS15 |
| F | SER16 |
| F | THR17 |
| F | ASN185 |
| F | PRO212 |
| F | ARG213 |
| F | ASP214 |
| F | GLN218 |
| F | GLU221 |
| F | MG292 |
| F | ALF293 |
| site_id | CC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SF4 G 290 |
| Chain | Residue |
| C | LEU158 |
| C | ILE159 |
| D | VAL157 |
| G | CYS97 |
| G | ALA98 |
| G | GLY99 |
| G | VAL131 |
| G | CYS132 |
| H | CYS97 |
| H | ALA98 |
| H | GLY99 |
| H | VAL131 |
| H | CYS132 |
| site_id | CC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADP G 291 |
| Chain | Residue |
| G | GLY12 |
| G | ILE13 |
| G | GLY14 |
| G | LYS15 |
| G | SER16 |
| G | THR17 |
| G | ASN185 |
| G | PRO212 |
| G | ARG213 |
| G | ASP214 |
| G | GLN218 |
| G | GLU221 |
| G | MG292 |
| G | ALF293 |
| H | LYS10 |
| H | GLU154 |
| H | MET156 |
| site_id | CC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADP H 291 |
| Chain | Residue |
| G | LYS10 |
| G | GLU154 |
| G | MET156 |
| H | GLY12 |
| H | ILE13 |
| H | GLY14 |
| H | LYS15 |
| H | SER16 |
| H | THR17 |
| H | ASN185 |
| H | PRO212 |
| H | ARG213 |
| H | ASP214 |
| H | GLN218 |
| H | GLU221 |
| H | MG292 |
| H | ALF293 |
Functional Information from PROSITE/UniProt
| site_id | PS00090 |
| Number of Residues | 15 |
| Details | NITROGENASE_1_2 Nitrogenases component 1 alpha and beta subunits signature 2. SECpigliGDDIeSV |
| Chain | Residue | Details |
| A | SER152-VAL166 | |
| B | THR151-PHE165 |
| site_id | PS00692 |
| Number of Residues | 14 |
| Details | NIFH_FRXC_2 NifH/frxC family signature 2. DvLGDVVCGGFAmP |
| Chain | Residue | Details |
| E | ASP125-PRO138 |
| site_id | PS00699 |
| Number of Residues | 8 |
| Details | NITROGENASE_1_1 Nitrogenases component 1 alpha and beta subunits signature 1. ISHGPVGC |
| Chain | Residue | Details |
| A | ILE81-CYS88 | |
| B | TYR88-CYS95 |
| site_id | PS00746 |
| Number of Residues | 13 |
| Details | NIFH_FRXC_1 NifH/frxC family signature 1. EsGGPepGvGCAG |
| Chain | Residue | Details |
| E | GLU87-GLY99 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| E | LYS10 | |
| H | LYS10 | |
| H | ALA98 | |
| H | GLY133 | |
| E | ALA98 | |
| E | GLY133 | |
| F | LYS10 | |
| F | ALA98 | |
| F | GLY133 | |
| G | LYS10 | |
| G | ALA98 | |
| G | GLY133 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase => ECO:0000250 |
| Chain | Residue | Details |
| E | GLY101 | |
| F | GLY101 | |
| G | GLY101 | |
| H | GLY101 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 10 |
| Details |
| Chain | Residue | Details |
| F | LYS15 | |
| E | ASP129 | |
| F | LYS41 | |
| A | HIS195 | |
| A | CYS62 | |
| A | ALA65 | |
| A | ARG96 | |
| B | VAL157 | |
| B | CYS153 | |
| E | LYS10 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| H | LYS10 | |
| H | ASP129 |
| site_id | CSA11 |
| Number of Residues | 10 |
| Details |
| Chain | Residue | Details |
| F | LYS15 | |
| E | ASP129 | |
| F | LYS41 | |
| A | HIS195 | |
| A | CYS62 | |
| A | ALA65 | |
| A | ARG96 | |
| B | VAL157 | |
| B | CYS153 | |
| E | LYS10 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| E | LYS15 | |
| E | LYS41 |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| G | LYS15 | |
| G | LYS41 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| H | LYS15 | |
| H | LYS41 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details |
| Chain | Residue | Details |
| C | HIS195 | |
| C | CYS62 | |
| C | ARG96 | |
| C | ALA65 |
| site_id | CSA3 |
| Number of Residues | 10 |
| Details |
| Chain | Residue | Details |
| F | LYS15 | |
| E | ASP129 | |
| F | LYS41 | |
| A | HIS195 | |
| A | CYS62 | |
| A | ALA65 | |
| A | ARG96 | |
| B | VAL157 | |
| B | CYS153 | |
| E | LYS10 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| D | VAL157 | |
| D | CYS153 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| A | CYS154 | |
| A | LEU158 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| C | CYS154 | |
| C | LEU158 |
| site_id | CSA7 |
| Number of Residues | 10 |
| Details |
| Chain | Residue | Details |
| F | LYS15 | |
| E | ASP129 | |
| F | LYS41 | |
| A | HIS195 | |
| A | CYS62 | |
| A | ALA65 | |
| A | ARG96 | |
| B | VAL157 | |
| B | CYS153 | |
| E | LYS10 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| F | LYS10 | |
| F | ASP129 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| G | LYS10 | |
| G | ASP129 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 212 |
| Chain | Residue | Details |
| E | GLY11 | electrostatic stabiliser, hydrogen bond donor |
| E | SER16 | electrostatic stabiliser, hydrogen bond donor |
| E | ALA42 | electrostatic stabiliser, hydrogen bond donor |
| E | 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 |
| F | GLY11 | electrostatic stabiliser, hydrogen bond donor |
| F | SER16 | electrostatic stabiliser, hydrogen bond donor |
| F | ALA42 | electrostatic stabiliser, hydrogen bond donor |
| F | VAL130 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 212 |
| Chain | Residue | Details |
| G | GLY11 | electrostatic stabiliser, hydrogen bond donor |
| G | SER16 | electrostatic stabiliser, hydrogen bond donor |
| G | ALA42 | electrostatic stabiliser, hydrogen bond donor |
| G | VAL130 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 212 |
| Chain | Residue | Details |
| H | GLY11 | electrostatic stabiliser, hydrogen bond donor |
| H | SER16 | electrostatic stabiliser, hydrogen bond donor |
| H | ALA42 | electrostatic stabiliser, hydrogen bond donor |
| H | VAL130 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
