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 |