1M34
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 |
| I | 0005524 | molecular_function | ATP binding |
| I | 0009399 | biological_process | nitrogen fixation |
| I | 0016163 | molecular_function | nitrogenase activity |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0016612 | cellular_component | molybdenum-iron nitrogenase complex |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0051536 | molecular_function | iron-sulfur cluster binding |
| J | 0005524 | molecular_function | ATP binding |
| J | 0009399 | biological_process | nitrogen fixation |
| J | 0016163 | molecular_function | nitrogenase activity |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0016612 | cellular_component | molybdenum-iron nitrogenase complex |
| J | 0046872 | molecular_function | metal ion binding |
| J | 0051536 | molecular_function | iron-sulfur cluster binding |
| K | 0005524 | molecular_function | ATP binding |
| K | 0009399 | biological_process | nitrogen fixation |
| K | 0016163 | molecular_function | nitrogenase activity |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0016612 | cellular_component | molybdenum-iron nitrogenase complex |
| K | 0046872 | molecular_function | metal ion binding |
| K | 0051536 | molecular_function | iron-sulfur cluster binding |
| L | 0005524 | molecular_function | ATP binding |
| L | 0009399 | biological_process | nitrogen fixation |
| L | 0016163 | molecular_function | nitrogenase activity |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0016612 | cellular_component | molybdenum-iron nitrogenase complex |
| L | 0046872 | molecular_function | metal ion binding |
| L | 0051536 | molecular_function | iron-sulfur cluster binding |
| M | 0005524 | molecular_function | ATP binding |
| M | 0009399 | biological_process | nitrogen fixation |
| M | 0016163 | molecular_function | nitrogenase activity |
| M | 0016491 | molecular_function | oxidoreductase activity |
| M | 0046872 | molecular_function | metal ion binding |
| M | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| N | 0005524 | molecular_function | ATP binding |
| N | 0009399 | biological_process | nitrogen fixation |
| N | 0016163 | molecular_function | nitrogenase activity |
| N | 0016491 | molecular_function | oxidoreductase activity |
| N | 0046872 | molecular_function | metal ion binding |
| N | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| O | 0005524 | molecular_function | ATP binding |
| O | 0009399 | biological_process | nitrogen fixation |
| O | 0016163 | molecular_function | nitrogenase activity |
| O | 0016491 | molecular_function | oxidoreductase activity |
| O | 0046872 | molecular_function | metal ion binding |
| O | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| P | 0005524 | molecular_function | ATP binding |
| P | 0009399 | biological_process | nitrogen fixation |
| P | 0016163 | molecular_function | nitrogenase activity |
| P | 0016491 | molecular_function | oxidoreductase activity |
| P | 0046872 | molecular_function | metal ion binding |
| P | 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 2099 |
| Chain | Residue |
| B | ARG108 |
| B | GLU109 |
| D | ASP353 |
| D | ASP357 |
| D | HOH2469 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 2299 |
| Chain | Residue |
| D | GLU109 |
| B | ASP353 |
| B | ASP357 |
| B | HOH2477 |
| D | ARG108 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG E 3092 |
| Chain | Residue |
| E | SER16 |
| E | ADP3091 |
| E | ALF3093 |
| E | HOH3131 |
| E | HOH3132 |
| E | HOH3133 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ALF E 3093 |
| Chain | Residue |
| E | GLY11 |
| E | GLY12 |
| E | LYS15 |
| E | ASP39 |
| E | LYS41 |
| E | LEU127 |
| E | GLY128 |
| E | ADP3091 |
| E | MG3092 |
| E | HOH3130 |
| E | HOH3131 |
| F | LYS10 |
| F | GLY11 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 3192 |
| Chain | Residue |
| F | SER16 |
| F | ADP3191 |
| F | ALF3193 |
| F | HOH3196 |
| F | HOH3197 |
| F | HOH3198 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ALF F 3193 |
| Chain | Residue |
| E | LYS10 |
| E | GLY11 |
| E | HOH3134 |
| F | GLY11 |
| F | GLY12 |
| F | LYS15 |
| F | ASP39 |
| F | LYS41 |
| F | GLY128 |
| F | ADP3191 |
| F | MG3192 |
| F | HOH3196 |
| F | HOH3197 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG G 3292 |
| Chain | Residue |
| G | SER16 |
| G | ADP3291 |
| G | ALF3293 |
| G | HOH3346 |
| G | HOH3347 |
| G | HOH3348 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ALF G 3293 |
| Chain | Residue |
| G | GLY11 |
| G | GLY12 |
| G | LYS15 |
| G | ASP39 |
| G | LYS41 |
| G | GLY128 |
| G | ADP3291 |
| G | MG3292 |
| G | HOH3345 |
| G | HOH3347 |
| H | LYS10 |
| H | GLY11 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG H 3392 |
| Chain | Residue |
| H | SER16 |
| H | ADP3391 |
| H | ALF3393 |
| H | HOH3417 |
| H | HOH3418 |
| H | HOH3419 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ALF H 3393 |
| Chain | Residue |
| G | LYS10 |
| G | GLY11 |
| G | HOH3349 |
| H | GLY11 |
| H | GLY12 |
| H | LYS15 |
| H | ASP39 |
| H | LYS41 |
| H | GLY128 |
| H | ADP3391 |
| H | MG3392 |
| H | HOH3418 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA L 4099 |
| Chain | Residue |
| J | ARG108 |
| J | GLU109 |
| J | HOH4505 |
| L | ASP353 |
| L | ASP357 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA J 4299 |
| Chain | Residue |
| J | ASP353 |
| J | ASP357 |
| J | HOH4506 |
| L | ARG108 |
| L | GLU109 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG M 5092 |
| Chain | Residue |
| M | HOH5154 |
| M | SER16 |
| M | ADP5091 |
| M | ALF5093 |
| M | HOH5152 |
| M | HOH5153 |
| site_id | BC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ALF M 5093 |
| Chain | Residue |
| M | GLY11 |
| M | GLY12 |
| M | LYS15 |
| M | ASP39 |
| M | LYS41 |
| M | LEU127 |
| M | GLY128 |
| M | ADP5091 |
| M | MG5092 |
| M | HOH5151 |
| M | HOH5152 |
| M | HOH5153 |
| N | LYS10 |
| N | GLY11 |
| N | HOH5202 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG N 5192 |
| Chain | Residue |
| N | SER16 |
| N | ADP5191 |
| N | ALF5193 |
| N | HOH5232 |
| N | HOH5233 |
| N | HOH5234 |
| site_id | BC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ALF N 5193 |
| Chain | Residue |
| M | LYS10 |
| M | GLY11 |
| M | HOH5102 |
| M | HOH5155 |
| N | GLY11 |
| N | GLY12 |
| N | LYS15 |
| N | ASP39 |
| N | LYS41 |
| N | LEU127 |
| N | GLY128 |
| N | ADP5191 |
| N | MG5192 |
| N | HOH5232 |
| N | HOH5233 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG O 5292 |
| Chain | Residue |
| O | SER16 |
| O | ADP5291 |
| O | ALF5293 |
| O | HOH5296 |
| O | HOH5297 |
| O | HOH5298 |
| site_id | BC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ALF O 5293 |
| Chain | Residue |
| O | GLY11 |
| O | GLY12 |
| O | LYS15 |
| O | LYS41 |
| O | LEU127 |
| O | GLY128 |
| O | ADP5291 |
| O | MG5292 |
| O | HOH5294 |
| O | HOH5296 |
| P | LYS10 |
| P | GLY11 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG P 5392 |
| Chain | Residue |
| P | SER16 |
| P | ADP5391 |
| P | ALF5393 |
| P | HOH5396 |
| P | HOH5397 |
| P | HOH5398 |
| site_id | CC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ALF P 5393 |
| Chain | Residue |
| O | LYS10 |
| O | GLY11 |
| O | ASP129 |
| O | HOH5394 |
| P | GLY11 |
| P | GLY12 |
| P | LYS15 |
| P | LYS41 |
| P | GLY128 |
| P | ADP5391 |
| P | MG5392 |
| site_id | CC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HCA A 2094 |
| Chain | Residue |
| A | ALA65 |
| A | GLY95 |
| A | GLN191 |
| A | GLY424 |
| A | ILE425 |
| A | LYS426 |
| A | HIS442 |
| A | CFM2096 |
| A | HOH2097 |
| A | HOH2106 |
| A | HOH2113 |
| A | HOH2131 |
| A | HOH2132 |
| A | HOH2138 |
| A | HOH2224 |
| site_id | CC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CFM A 2096 |
| Chain | Residue |
| A | ARG96 |
| A | HIS195 |
| A | TYR229 |
| A | ILE231 |
| A | CYS275 |
| A | ILE355 |
| A | GLY356 |
| A | GLY357 |
| A | ARG359 |
| A | PHE381 |
| A | HIS442 |
| A | HCA2094 |
| site_id | CC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CLF B 2098 |
| Chain | Residue |
| A | CYS62 |
| A | TYR64 |
| A | VAL86 |
| A | CYS88 |
| A | TYR91 |
| A | CYS154 |
| A | GLY185 |
| B | CYS70 |
| B | PRO72 |
| B | SER92 |
| B | CYS95 |
| B | TYR98 |
| B | CYS153 |
| B | SER188 |
| site_id | CC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HCA C 2294 |
| Chain | Residue |
| C | ARG96 |
| C | GLN191 |
| C | GLY424 |
| C | ILE425 |
| C | LYS426 |
| C | HIS442 |
| C | CFM2296 |
| C | HOH2306 |
| C | HOH2339 |
| C | HOH2379 |
| C | HOH2381 |
| C | HOH2386 |
| C | HOH2397 |
| C | HOH2414 |
| site_id | CC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CFM C 2296 |
| Chain | Residue |
| C | ARG96 |
| C | HIS195 |
| C | TYR229 |
| C | CYS275 |
| C | SER278 |
| C | GLY356 |
| C | GLY357 |
| C | LEU358 |
| C | ARG359 |
| C | PHE381 |
| C | HIS442 |
| C | HCA2294 |
| site_id | CC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CLF D 2298 |
| Chain | Residue |
| C | CYS62 |
| C | TYR64 |
| C | PRO85 |
| C | VAL86 |
| C | CYS88 |
| C | CYS154 |
| C | GLY185 |
| D | CYS70 |
| D | PRO72 |
| D | SER92 |
| D | CYS95 |
| D | TYR98 |
| D | CYS153 |
| D | SER188 |
| site_id | CC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 E 3090 |
| Chain | Residue |
| A | LEU158 |
| B | VAL157 |
| E | CYS97 |
| E | ALA98 |
| E | GLY99 |
| E | CYS132 |
| F | CYS97 |
| F | ALA98 |
| F | GLY99 |
| F | CYS132 |
| site_id | DC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP E 3091 |
| Chain | Residue |
| E | GLY12 |
| E | ILE13 |
| E | GLY14 |
| E | LYS15 |
| E | SER16 |
| E | THR17 |
| E | ASN185 |
| E | PRO212 |
| E | ARG213 |
| E | ASP214 |
| E | VAL217 |
| E | GLN218 |
| E | GLU221 |
| E | GLN236 |
| E | MG3092 |
| E | ALF3093 |
| E | HOH3132 |
| F | LYS10 |
| F | GLU154 |
| F | MET156 |
| site_id | DC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ADP F 3191 |
| Chain | Residue |
| E | LYS10 |
| E | GLU154 |
| E | MET156 |
| F | GLY12 |
| F | ILE13 |
| F | GLY14 |
| F | LYS15 |
| F | SER16 |
| F | THR17 |
| F | ASN185 |
| F | VAL211 |
| F | PRO212 |
| F | ARG213 |
| F | ASP214 |
| F | VAL217 |
| F | GLN218 |
| F | GLU221 |
| F | GLN236 |
| F | TYR240 |
| F | HOH1505 |
| F | MG3192 |
| F | ALF3193 |
| F | HOH3196 |
| F | HOH3197 |
| site_id | DC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 G 3290 |
| Chain | Residue |
| C | LEU158 |
| D | VAL157 |
| D | ILE158 |
| G | CYS97 |
| G | ALA98 |
| G | GLY99 |
| G | CYS132 |
| H | CYS97 |
| H | ALA98 |
| H | GLY99 |
| H | CYS132 |
| site_id | DC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADP G 3291 |
| Chain | Residue |
| G | GLY12 |
| G | ILE13 |
| G | GLY14 |
| G | LYS15 |
| G | SER16 |
| G | THR17 |
| G | ASN185 |
| G | VAL211 |
| G | PRO212 |
| G | ARG213 |
| G | ASP214 |
| G | GLN218 |
| G | GLU221 |
| G | GLN236 |
| G | MG3292 |
| G | ALF3293 |
| G | HOH3346 |
| G | HOH3347 |
| H | LYS10 |
| H | GLU154 |
| H | MET156 |
| site_id | DC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADP H 3391 |
| 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 | VAL217 |
| H | GLN218 |
| H | GLU221 |
| H | GLN236 |
| H | MG3392 |
| H | ALF3393 |
| H | HOH3402 |
| H | HOH3417 |
| site_id | DC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HCA I 4094 |
| Chain | Residue |
| I | ALA65 |
| I | ARG96 |
| I | GLN191 |
| I | GLY424 |
| I | ILE425 |
| I | LYS426 |
| I | HIS442 |
| I | CFM4096 |
| I | HOH4107 |
| I | HOH4109 |
| I | HOH4147 |
| I | HOH4150 |
| I | HOH4194 |
| I | HOH4204 |
| I | HOH4225 |
| I | HOH4286 |
| J | HOH4361 |
| site_id | DC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CFM I 4096 |
| Chain | Residue |
| I | ARG96 |
| I | HIS195 |
| I | TYR229 |
| I | CYS275 |
| I | GLY356 |
| I | GLY357 |
| I | LEU358 |
| I | ARG359 |
| I | PHE381 |
| I | HIS442 |
| I | HCA4094 |
| site_id | DC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CLF J 4098 |
| Chain | Residue |
| I | CYS62 |
| I | TYR64 |
| I | PRO85 |
| I | VAL86 |
| I | CYS88 |
| I | CYS154 |
| I | GLY185 |
| J | CYS70 |
| J | PRO72 |
| J | SER92 |
| J | CYS95 |
| J | TYR98 |
| J | CYS153 |
| J | SER188 |
| site_id | DC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HCA K 4294 |
| Chain | Residue |
| K | ALA65 |
| K | GLN191 |
| K | ILE425 |
| K | LYS426 |
| K | HIS442 |
| K | CFM4296 |
| K | HOH4299 |
| K | HOH4304 |
| K | HOH4363 |
| K | HOH4398 |
| L | HOH4368 |
| site_id | EC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CFM K 4296 |
| Chain | Residue |
| K | ARG96 |
| K | HIS195 |
| K | TYR229 |
| K | CYS275 |
| K | GLY356 |
| K | GLY357 |
| K | LEU358 |
| K | ARG359 |
| K | PHE381 |
| K | HIS442 |
| K | HCA4294 |
| site_id | EC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CLF L 4298 |
| Chain | Residue |
| K | CYS62 |
| K | TYR64 |
| K | PRO85 |
| K | VAL86 |
| K | CYS88 |
| K | TYR91 |
| K | CYS154 |
| K | GLY185 |
| L | CYS70 |
| L | PRO72 |
| L | SER92 |
| L | CYS95 |
| L | TYR98 |
| L | CYS153 |
| L | SER188 |
| site_id | EC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 M 5090 |
| Chain | Residue |
| I | LEU158 |
| J | VAL157 |
| M | CYS97 |
| M | ALA98 |
| M | GLY99 |
| M | CYS132 |
| N | CYS97 |
| N | ALA98 |
| N | GLY99 |
| N | VAL131 |
| N | CYS132 |
| site_id | EC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADP M 5091 |
| Chain | Residue |
| M | GLY12 |
| M | ILE13 |
| M | GLY14 |
| M | LYS15 |
| M | SER16 |
| M | THR17 |
| M | ASN185 |
| M | PRO212 |
| M | ARG213 |
| M | ASP214 |
| M | GLN218 |
| M | GLU221 |
| M | GLN236 |
| M | MG5092 |
| M | ALF5093 |
| M | HOH5113 |
| M | HOH5152 |
| M | HOH5153 |
| N | LYS10 |
| N | GLU154 |
| N | MET156 |
| site_id | EC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADP N 5191 |
| Chain | Residue |
| M | LYS10 |
| M | GLU154 |
| M | MET156 |
| N | GLY12 |
| N | ILE13 |
| N | GLY14 |
| N | LYS15 |
| N | SER16 |
| N | THR17 |
| N | ASN185 |
| N | PRO212 |
| N | ARG213 |
| N | ASP214 |
| N | GLN218 |
| N | GLU221 |
| N | GLN236 |
| N | MG5192 |
| N | ALF5193 |
| N | HOH5206 |
| N | HOH5232 |
| N | HOH5233 |
| site_id | EC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 O 5290 |
| Chain | Residue |
| K | LEU158 |
| L | VAL157 |
| O | CYS97 |
| O | ALA98 |
| O | GLY99 |
| O | CYS132 |
| P | CYS97 |
| P | ALA98 |
| P | GLY99 |
| P | CYS132 |
| site_id | EC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ADP O 5291 |
| Chain | Residue |
| O | GLY12 |
| O | ILE13 |
| O | GLY14 |
| O | LYS15 |
| O | SER16 |
| O | THR17 |
| O | ASN185 |
| O | PRO212 |
| O | ARG213 |
| O | ASP214 |
| O | VAL217 |
| O | GLN218 |
| O | GLU221 |
| O | GLN236 |
| O | HOH1451 |
| O | MG5292 |
| O | ALF5293 |
| O | HOH5296 |
| P | LYS10 |
| P | GLU154 |
| P | MET155 |
| P | MET156 |
| site_id | EC8 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ADP P 5391 |
| Chain | Residue |
| O | LYS10 |
| O | GLU154 |
| O | MET156 |
| P | GLY12 |
| P | ILE13 |
| P | GLY14 |
| P | LYS15 |
| P | SER16 |
| P | THR17 |
| P | ASN185 |
| P | VAL211 |
| P | PRO212 |
| P | ARG213 |
| P | ASP214 |
| P | VAL217 |
| P | GLN218 |
| P | GLU221 |
| P | GLN236 |
| P | TYR240 |
| P | MG5392 |
| P | ALF5393 |
| P | HOH5396 |
| P | HOH5397 |
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 | 24 |
| Details | BINDING: |
| Chain | Residue | Details |
| E | GLY9 | |
| H | GLY9 | |
| H | CYS97 | |
| H | CYS132 | |
| M | GLY9 | |
| M | CYS97 | |
| M | CYS132 | |
| N | GLY9 | |
| N | CYS97 | |
| N | CYS132 | |
| O | GLY9 | |
| E | CYS97 | |
| O | CYS97 | |
| O | CYS132 | |
| P | GLY9 | |
| P | CYS97 | |
| P | CYS132 | |
| E | CYS132 | |
| F | GLY9 | |
| F | CYS97 | |
| F | CYS132 | |
| G | GLY9 | |
| G | CYS97 | |
| G | CYS132 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | MOD_RES: ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase => ECO:0000250 |
| Chain | Residue | Details |
| E | ARG100 | |
| F | ARG100 | |
| G | ARG100 | |
| H | ARG100 | |
| M | ARG100 | |
| N | ARG100 | |
| O | ARG100 | |
| P | ARG100 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1f48 |
| Chain | Residue | Details |
| E | LYS15 | |
| E | GLY12 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1f48 |
| Chain | Residue | Details |
| F | LYS15 | |
| F | GLY12 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1f48 |
| Chain | Residue | Details |
| G | LYS15 | |
| G | GLY12 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1f48 |
| Chain | Residue | Details |
| H | LYS15 | |
| H | GLY12 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1f48 |
| Chain | Residue | Details |
| M | LYS15 | |
| M | GLY12 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1f48 |
| Chain | Residue | Details |
| N | LYS15 | |
| N | GLY12 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1f48 |
| Chain | Residue | Details |
| O | LYS15 | |
| O | GLY12 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1f48 |
| Chain | Residue | Details |
| P | LYS15 | |
| P | GLY12 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 212 |
| Chain | Residue | Details |
| E | LYS10 | electrostatic stabiliser, hydrogen bond donor |
| E | LYS15 | electrostatic stabiliser, hydrogen bond donor |
| E | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| E | 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 |
| F | LYS10 | electrostatic stabiliser, hydrogen bond donor |
| F | LYS15 | electrostatic stabiliser, hydrogen bond donor |
| F | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| F | ASP129 | 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 | LYS10 | electrostatic stabiliser, hydrogen bond donor |
| G | LYS15 | electrostatic stabiliser, hydrogen bond donor |
| G | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| G | ASP129 | 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 | LYS10 | electrostatic stabiliser, hydrogen bond donor |
| H | LYS15 | electrostatic stabiliser, hydrogen bond donor |
| H | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| H | ASP129 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA5 |
| Number of Residues | 4 |
| Details | M-CSA 212 |
| Chain | Residue | Details |
| M | LYS10 | electrostatic stabiliser, hydrogen bond donor |
| M | LYS15 | electrostatic stabiliser, hydrogen bond donor |
| M | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| M | ASP129 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA6 |
| Number of Residues | 4 |
| Details | M-CSA 212 |
| Chain | Residue | Details |
| N | LYS10 | electrostatic stabiliser, hydrogen bond donor |
| N | LYS15 | electrostatic stabiliser, hydrogen bond donor |
| N | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| N | ASP129 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA7 |
| Number of Residues | 4 |
| Details | M-CSA 212 |
| Chain | Residue | Details |
| O | LYS10 | electrostatic stabiliser, hydrogen bond donor |
| O | LYS15 | electrostatic stabiliser, hydrogen bond donor |
| O | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| O | ASP129 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA8 |
| Number of Residues | 4 |
| Details | M-CSA 212 |
| Chain | Residue | Details |
| P | LYS10 | electrostatic stabiliser, hydrogen bond donor |
| P | LYS15 | electrostatic stabiliser, hydrogen bond donor |
| P | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| P | ASP129 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
