1FPY
CRYSTAL STRUCTURE OF GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM WITH INHIBITOR PHOSPHINOTHRICIN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004356 | molecular_function | glutamine synthetase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006542 | biological_process | glutamine biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016874 | molecular_function | ligase activity |
| A | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| A | 0019740 | biological_process | nitrogen utilization |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051260 | biological_process | protein homooligomerization |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004356 | molecular_function | glutamine synthetase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006542 | biological_process | glutamine biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016874 | molecular_function | ligase activity |
| B | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| B | 0019740 | biological_process | nitrogen utilization |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051260 | biological_process | protein homooligomerization |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004356 | molecular_function | glutamine synthetase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006542 | biological_process | glutamine biosynthetic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016874 | molecular_function | ligase activity |
| C | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| C | 0019740 | biological_process | nitrogen utilization |
| C | 0030145 | molecular_function | manganese ion binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051260 | biological_process | protein homooligomerization |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004356 | molecular_function | glutamine synthetase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006542 | biological_process | glutamine biosynthetic process |
| D | 0016020 | cellular_component | membrane |
| D | 0016874 | molecular_function | ligase activity |
| D | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| D | 0019740 | biological_process | nitrogen utilization |
| D | 0030145 | molecular_function | manganese ion binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051260 | biological_process | protein homooligomerization |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004356 | molecular_function | glutamine synthetase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006542 | biological_process | glutamine biosynthetic process |
| E | 0016020 | cellular_component | membrane |
| E | 0016874 | molecular_function | ligase activity |
| E | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| E | 0019740 | biological_process | nitrogen utilization |
| E | 0030145 | molecular_function | manganese ion binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051260 | biological_process | protein homooligomerization |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004356 | molecular_function | glutamine synthetase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006542 | biological_process | glutamine biosynthetic process |
| F | 0016020 | cellular_component | membrane |
| F | 0016874 | molecular_function | ligase activity |
| F | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| F | 0019740 | biological_process | nitrogen utilization |
| F | 0030145 | molecular_function | manganese ion binding |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051260 | biological_process | protein homooligomerization |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0004356 | molecular_function | glutamine synthetase activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0006542 | biological_process | glutamine biosynthetic process |
| G | 0016020 | cellular_component | membrane |
| G | 0016874 | molecular_function | ligase activity |
| G | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| G | 0019740 | biological_process | nitrogen utilization |
| G | 0030145 | molecular_function | manganese ion binding |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0051260 | biological_process | protein homooligomerization |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0004356 | molecular_function | glutamine synthetase activity |
| H | 0005524 | molecular_function | ATP binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0006542 | biological_process | glutamine biosynthetic process |
| H | 0016020 | cellular_component | membrane |
| H | 0016874 | molecular_function | ligase activity |
| H | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| H | 0019740 | biological_process | nitrogen utilization |
| H | 0030145 | molecular_function | manganese ion binding |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0051260 | biological_process | protein homooligomerization |
| I | 0003824 | molecular_function | catalytic activity |
| I | 0004356 | molecular_function | glutamine synthetase activity |
| I | 0005524 | molecular_function | ATP binding |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0006542 | biological_process | glutamine biosynthetic process |
| I | 0016020 | cellular_component | membrane |
| I | 0016874 | molecular_function | ligase activity |
| I | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| I | 0019740 | biological_process | nitrogen utilization |
| I | 0030145 | molecular_function | manganese ion binding |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0051260 | biological_process | protein homooligomerization |
| J | 0003824 | molecular_function | catalytic activity |
| J | 0004356 | molecular_function | glutamine synthetase activity |
| J | 0005524 | molecular_function | ATP binding |
| J | 0005737 | cellular_component | cytoplasm |
| J | 0006542 | biological_process | glutamine biosynthetic process |
| J | 0016020 | cellular_component | membrane |
| J | 0016874 | molecular_function | ligase activity |
| J | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| J | 0019740 | biological_process | nitrogen utilization |
| J | 0030145 | molecular_function | manganese ion binding |
| J | 0046872 | molecular_function | metal ion binding |
| J | 0051260 | biological_process | protein homooligomerization |
| K | 0003824 | molecular_function | catalytic activity |
| K | 0004356 | molecular_function | glutamine synthetase activity |
| K | 0005524 | molecular_function | ATP binding |
| K | 0005737 | cellular_component | cytoplasm |
| K | 0006542 | biological_process | glutamine biosynthetic process |
| K | 0016020 | cellular_component | membrane |
| K | 0016874 | molecular_function | ligase activity |
| K | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| K | 0019740 | biological_process | nitrogen utilization |
| K | 0030145 | molecular_function | manganese ion binding |
| K | 0046872 | molecular_function | metal ion binding |
| K | 0051260 | biological_process | protein homooligomerization |
| L | 0003824 | molecular_function | catalytic activity |
| L | 0004356 | molecular_function | glutamine synthetase activity |
| L | 0005524 | molecular_function | ATP binding |
| L | 0005737 | cellular_component | cytoplasm |
| L | 0006542 | biological_process | glutamine biosynthetic process |
| L | 0016020 | cellular_component | membrane |
| L | 0016874 | molecular_function | ligase activity |
| L | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| L | 0019740 | biological_process | nitrogen utilization |
| L | 0030145 | molecular_function | manganese ion binding |
| L | 0046872 | molecular_function | metal ion binding |
| L | 0051260 | biological_process | protein homooligomerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 469 |
| Chain | Residue |
| A | GLU131 |
| A | GLU212 |
| A | GLU220 |
| A | PPQ5900 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 470 |
| Chain | Residue |
| A | GLU129 |
| A | HIS269 |
| A | GLU357 |
| A | ADP4471 |
| A | PPQ5900 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN B 469 |
| Chain | Residue |
| B | GLU131 |
| B | GLU212 |
| B | GLU220 |
| B | PPQ5901 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 470 |
| Chain | Residue |
| B | GLU129 |
| B | HIS269 |
| B | GLU357 |
| B | ADP4472 |
| B | PPQ5901 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN C 469 |
| Chain | Residue |
| C | GLU131 |
| C | GLU212 |
| C | GLU220 |
| C | PPQ5902 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 470 |
| Chain | Residue |
| C | GLU129 |
| C | HIS269 |
| C | GLU357 |
| C | ADP4473 |
| C | PPQ5902 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN D 469 |
| Chain | Residue |
| D | GLU131 |
| D | GLU212 |
| D | GLU220 |
| D | PPQ5903 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN D 470 |
| Chain | Residue |
| D | GLU129 |
| D | HIS269 |
| D | GLU357 |
| D | ADP4474 |
| D | PPQ5903 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN E 469 |
| Chain | Residue |
| E | GLU131 |
| E | GLU212 |
| E | GLU220 |
| E | PPQ5904 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN E 470 |
| Chain | Residue |
| E | GLU129 |
| E | HIS269 |
| E | GLU357 |
| E | ADP4475 |
| E | PPQ5904 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN F 469 |
| Chain | Residue |
| F | GLU131 |
| F | GLU212 |
| F | GLU220 |
| F | PPQ5905 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN F 470 |
| Chain | Residue |
| F | GLU129 |
| F | HIS269 |
| F | GLU357 |
| F | ADP4476 |
| F | PPQ5905 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN G 469 |
| Chain | Residue |
| G | GLU131 |
| G | GLU212 |
| G | GLU220 |
| G | PPQ5906 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN G 470 |
| Chain | Residue |
| G | GLU129 |
| G | HIS269 |
| G | GLU357 |
| G | ADP4477 |
| G | PPQ5906 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN H 469 |
| Chain | Residue |
| H | GLU131 |
| H | GLU212 |
| H | GLU220 |
| H | PPQ5907 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN H 470 |
| Chain | Residue |
| H | GLU129 |
| H | HIS269 |
| H | GLU357 |
| H | ADP4478 |
| H | PPQ5907 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN I 469 |
| Chain | Residue |
| I | GLU131 |
| I | GLU212 |
| I | GLU220 |
| I | PPQ5908 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN I 470 |
| Chain | Residue |
| I | GLU129 |
| I | HIS269 |
| I | GLU357 |
| I | ADP4479 |
| I | PPQ5908 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN J 469 |
| Chain | Residue |
| J | GLU131 |
| J | GLU212 |
| J | GLU220 |
| J | PPQ5909 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN J 470 |
| Chain | Residue |
| J | GLU129 |
| J | HIS269 |
| J | GLU357 |
| J | ADP4480 |
| J | PPQ5909 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN K 469 |
| Chain | Residue |
| K | GLU131 |
| K | GLU212 |
| K | GLU220 |
| K | PPQ5910 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN K 470 |
| Chain | Residue |
| K | GLU129 |
| K | HIS269 |
| K | GLU357 |
| K | ADP4481 |
| K | PPQ5910 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN L 469 |
| Chain | Residue |
| L | GLU131 |
| L | GLU212 |
| L | GLU220 |
| L | PPQ5911 |
| site_id | CC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN L 470 |
| Chain | Residue |
| L | GLU129 |
| L | HIS269 |
| L | GLU357 |
| L | ADP4482 |
| L | PPQ5911 |
| site_id | CC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP A 4471 |
| Chain | Residue |
| A | GLY127 |
| A | GLU129 |
| A | GLU207 |
| A | THR223 |
| A | ARG224 |
| A | PHE225 |
| A | HIS271 |
| A | SER273 |
| A | ARG355 |
| A | GLU357 |
| A | MN470 |
| A | HOH5976 |
| A | HOH6045 |
| site_id | CC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP B 4472 |
| Chain | Residue |
| B | GLY127 |
| B | GLU129 |
| B | GLU207 |
| B | THR223 |
| B | ARG224 |
| B | PHE225 |
| B | HIS271 |
| B | SER273 |
| B | ARG355 |
| B | GLU357 |
| B | MN470 |
| B | HOH5977 |
| B | HOH6049 |
| site_id | CC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP C 4473 |
| Chain | Residue |
| C | GLY127 |
| C | GLU129 |
| C | GLU207 |
| C | THR223 |
| C | ARG224 |
| C | PHE225 |
| C | HIS271 |
| C | SER273 |
| C | ARG355 |
| C | GLU357 |
| C | MN470 |
| C | HOH5976 |
| C | HOH6046 |
| site_id | DC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP D 4474 |
| Chain | Residue |
| D | GLY127 |
| D | GLU129 |
| D | GLU207 |
| D | THR223 |
| D | ARG224 |
| D | PHE225 |
| D | HIS271 |
| D | SER273 |
| D | ARG355 |
| D | GLU357 |
| D | MN470 |
| D | HOH5979 |
| D | HOH6049 |
| site_id | DC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP E 4475 |
| Chain | Residue |
| E | GLY127 |
| E | GLU129 |
| E | GLU207 |
| E | THR223 |
| E | ARG224 |
| E | PHE225 |
| E | HIS271 |
| E | SER273 |
| E | ARG355 |
| E | GLU357 |
| E | MN470 |
| E | HOH691 |
| E | HOH849 |
| site_id | DC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP F 4476 |
| Chain | Residue |
| F | GLY127 |
| F | GLU129 |
| F | GLU207 |
| F | THR223 |
| F | ARG224 |
| F | PHE225 |
| F | HIS271 |
| F | SER273 |
| F | ARG355 |
| F | GLU357 |
| F | MN470 |
| F | HOH5908 |
| F | HOH5986 |
| site_id | DC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP G 4477 |
| Chain | Residue |
| G | GLY127 |
| G | GLU129 |
| G | GLU207 |
| G | THR223 |
| G | ARG224 |
| G | PHE225 |
| G | HIS271 |
| G | SER273 |
| G | ARG355 |
| G | GLU357 |
| G | MN470 |
| G | HOH5986 |
| G | HOH6058 |
| site_id | DC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP H 4478 |
| Chain | Residue |
| H | GLY127 |
| H | GLU129 |
| H | GLU207 |
| H | THR223 |
| H | ARG224 |
| H | PHE225 |
| H | HIS271 |
| H | SER273 |
| H | ARG355 |
| H | GLU357 |
| H | MN470 |
| H | HOH5914 |
| H | HOH5990 |
| site_id | DC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP I 4479 |
| Chain | Residue |
| I | GLY127 |
| I | GLU129 |
| I | GLU207 |
| I | THR223 |
| I | ARG224 |
| I | PHE225 |
| I | HIS271 |
| I | SER273 |
| I | ARG355 |
| I | GLU357 |
| I | MN470 |
| I | HOH5918 |
| I | HOH5997 |
| site_id | DC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP J 4480 |
| Chain | Residue |
| J | GLY127 |
| J | GLU129 |
| J | GLU207 |
| J | THR223 |
| J | ARG224 |
| J | PHE225 |
| J | HIS271 |
| J | SER273 |
| J | ARG355 |
| J | GLU357 |
| J | MN470 |
| J | HOH5916 |
| J | HOH5993 |
| site_id | DC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP K 4481 |
| Chain | Residue |
| K | GLY127 |
| K | GLU129 |
| K | GLU207 |
| K | THR223 |
| K | ARG224 |
| K | PHE225 |
| K | HIS271 |
| K | SER273 |
| K | ARG355 |
| K | GLU357 |
| K | MN470 |
| K | HOH1461 |
| K | HOH1609 |
| site_id | DC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP L 4482 |
| Chain | Residue |
| L | GLY127 |
| L | GLU129 |
| L | GLU207 |
| L | THR223 |
| L | ARG224 |
| L | PHE225 |
| L | HIS271 |
| L | SER273 |
| L | ARG355 |
| L | GLU357 |
| L | MN470 |
| L | HOH1614 |
| L | HOH1762 |
| site_id | EC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PPQ A 5900 |
| Chain | Residue |
| A | GLU131 |
| A | GLU212 |
| A | ASN264 |
| A | GLY265 |
| A | SER266 |
| A | GLY267 |
| A | HIS269 |
| A | ARG321 |
| A | GLU327 |
| A | ARG359 |
| A | MN469 |
| A | MN470 |
| site_id | EC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PPQ B 5901 |
| Chain | Residue |
| B | GLU131 |
| B | GLU212 |
| B | ASN264 |
| B | GLY265 |
| B | SER266 |
| B | GLY267 |
| B | HIS269 |
| B | ARG321 |
| B | GLU327 |
| B | ARG359 |
| B | MN469 |
| B | MN470 |
| site_id | EC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PPQ C 5902 |
| Chain | Residue |
| C | GLU131 |
| C | GLU212 |
| C | ASN264 |
| C | GLY265 |
| C | SER266 |
| C | GLY267 |
| C | HIS269 |
| C | ARG321 |
| C | GLU327 |
| C | ARG359 |
| C | MN469 |
| C | MN470 |
| site_id | EC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PPQ D 5903 |
| Chain | Residue |
| D | GLU131 |
| D | GLU212 |
| D | ASN264 |
| D | GLY265 |
| D | SER266 |
| D | GLY267 |
| D | HIS269 |
| D | ARG321 |
| D | GLU327 |
| D | ARG359 |
| D | MN469 |
| D | MN470 |
| site_id | EC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PPQ E 5904 |
| Chain | Residue |
| E | GLU131 |
| E | GLU212 |
| E | ASN264 |
| E | GLY265 |
| E | SER266 |
| E | GLY267 |
| E | HIS269 |
| E | ARG321 |
| E | GLU327 |
| E | ARG359 |
| E | MN469 |
| E | MN470 |
| site_id | EC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PPQ F 5905 |
| Chain | Residue |
| F | GLU131 |
| F | GLU212 |
| F | ASN264 |
| F | GLY265 |
| F | SER266 |
| F | GLY267 |
| F | HIS269 |
| F | ARG321 |
| F | GLU327 |
| F | ARG359 |
| F | MN469 |
| F | MN470 |
| site_id | EC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PPQ G 5906 |
| Chain | Residue |
| G | GLU131 |
| G | GLU212 |
| G | ASN264 |
| G | GLY265 |
| G | SER266 |
| G | GLY267 |
| G | HIS269 |
| G | ARG321 |
| G | GLU327 |
| G | ARG359 |
| G | MN469 |
| G | MN470 |
| site_id | EC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PPQ H 5907 |
| Chain | Residue |
| H | GLU131 |
| H | GLU212 |
| H | ASN264 |
| H | GLY265 |
| H | SER266 |
| H | GLY267 |
| H | HIS269 |
| H | ARG321 |
| H | GLU327 |
| H | ARG359 |
| H | MN469 |
| H | MN470 |
| site_id | EC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PPQ I 5908 |
| Chain | Residue |
| I | GLU131 |
| I | GLU212 |
| I | ASN264 |
| I | GLY265 |
| I | SER266 |
| I | GLY267 |
| I | HIS269 |
| I | ARG321 |
| I | GLU327 |
| I | ARG359 |
| I | MN469 |
| I | MN470 |
| site_id | FC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PPQ J 5909 |
| Chain | Residue |
| J | GLU131 |
| J | GLU212 |
| J | ASN264 |
| J | GLY265 |
| J | SER266 |
| J | GLY267 |
| J | HIS269 |
| J | ARG321 |
| J | GLU327 |
| J | ARG359 |
| J | MN469 |
| J | MN470 |
| site_id | FC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PPQ K 5910 |
| Chain | Residue |
| K | GLU131 |
| K | GLU212 |
| K | ASN264 |
| K | GLY265 |
| K | SER266 |
| K | GLY267 |
| K | HIS269 |
| K | ARG321 |
| K | GLU327 |
| K | ARG359 |
| K | MN469 |
| K | MN470 |
| site_id | FC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PPQ L 5911 |
| Chain | Residue |
| L | GLU131 |
| L | GLU212 |
| L | ASN264 |
| L | GLY265 |
| L | SER266 |
| L | GLY267 |
| L | HIS269 |
| L | ARG321 |
| L | GLU327 |
| L | ARG359 |
| L | MN469 |
| L | MN470 |
Functional Information from PROSITE/UniProt
| site_id | PS00180 |
| Number of Residues | 19 |
| Details | GLNA_1 Glutamine synthetase signature 1. FDGSSiggwkginESDmvL |
| Chain | Residue | Details |
| A | PHE49-LEU67 |
| site_id | PS00181 |
| Number of Residues | 16 |
| Details | GLNA_ATP Glutamine synthetase putative ATP-binding region signature. KPMfgd..NGSGmHchmS |
| Chain | Residue | Details |
| A | LYS258-SER273 |
| site_id | PS00182 |
| Number of Residues | 13 |
| Details | GLNA_ADENYLATION Glutamine synthetase class-I adenylation site. KIhpgepMDKNLY |
| Chain | Residue | Details |
| A | LYS385-TYR397 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11329256, ECO:0000269|PubMed:2572586, ECO:0000269|PubMed:8099447, ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1F52, ECO:0007744|PDB:1FPY, ECO:0007744|PDB:2GLS, ECO:0007744|PDB:2LGS |
| Chain | Residue | Details |
| A | PRO130 | |
| E | CYS270 | |
| F | PRO130 | |
| F | CYS270 | |
| G | PRO130 | |
| G | CYS270 | |
| H | PRO130 | |
| H | CYS270 | |
| I | PRO130 | |
| I | CYS270 | |
| J | PRO130 | |
| A | CYS270 | |
| J | CYS270 | |
| K | PRO130 | |
| K | CYS270 | |
| L | PRO130 | |
| L | CYS270 | |
| B | PRO130 | |
| B | CYS270 | |
| C | PRO130 | |
| C | CYS270 | |
| D | PRO130 | |
| D | CYS270 | |
| E | PRO130 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11329256, ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447, ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1F52, ECO:0007744|PDB:1FPY, ECO:0007744|PDB:1LGR, ECO:0007744|PDB:2LGS |
| Chain | Residue | Details |
| A | PHE132 | |
| D | PHE132 | |
| D | VAL213 | |
| D | VAL221 | |
| E | PHE132 | |
| E | VAL213 | |
| E | VAL221 | |
| F | PHE132 | |
| F | VAL213 | |
| F | VAL221 | |
| G | PHE132 | |
| A | VAL213 | |
| G | VAL213 | |
| G | VAL221 | |
| H | PHE132 | |
| H | VAL213 | |
| H | VAL221 | |
| I | PHE132 | |
| I | VAL213 | |
| I | VAL221 | |
| J | PHE132 | |
| J | VAL213 | |
| A | VAL221 | |
| J | VAL221 | |
| K | PHE132 | |
| K | VAL213 | |
| K | VAL221 | |
| L | PHE132 | |
| L | VAL213 | |
| L | VAL221 | |
| B | PHE132 | |
| B | VAL213 | |
| B | VAL221 | |
| C | PHE132 | |
| C | VAL213 | |
| C | VAL221 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7727369, ECO:0007744|PDB:1LGR |
| Chain | Residue | Details |
| A | ALA208 | |
| J | ALA208 | |
| K | ALA208 | |
| L | ALA208 | |
| B | ALA208 | |
| C | ALA208 | |
| D | ALA208 | |
| E | ALA208 | |
| F | ALA208 | |
| G | ALA208 | |
| H | ALA208 | |
| I | ALA208 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447, ECO:0000305|PubMed:11329256, ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1FPY, ECO:0007744|PDB:1LGR, ECO:0007744|PDB:2LGS |
| Chain | Residue | Details |
| A | GLY265 | |
| J | GLY265 | |
| K | GLY265 | |
| L | GLY265 | |
| B | GLY265 | |
| C | GLY265 | |
| D | GLY265 | |
| E | GLY265 | |
| F | GLY265 | |
| G | GLY265 | |
| H | GLY265 | |
| I | GLY265 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P12425 |
| Chain | Residue | Details |
| A | SER266 | |
| J | SER266 | |
| K | SER266 | |
| L | SER266 | |
| B | SER266 | |
| C | SER266 | |
| D | SER266 | |
| E | SER266 | |
| F | SER266 | |
| G | SER266 | |
| H | SER266 | |
| I | SER266 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11329256, ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1F52, ECO:0007744|PDB:1FPY |
| Chain | Residue | Details |
| A | MET272 | |
| J | MET272 | |
| K | MET272 | |
| L | MET272 | |
| B | MET272 | |
| C | MET272 | |
| D | MET272 | |
| E | MET272 | |
| F | MET272 | |
| G | MET272 | |
| H | MET272 | |
| I | MET272 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P77961 |
| Chain | Residue | Details |
| A | LEU274 | |
| E | ALA353 | |
| F | LEU274 | |
| F | ALA353 | |
| G | LEU274 | |
| G | ALA353 | |
| H | LEU274 | |
| H | ALA353 | |
| I | LEU274 | |
| I | ALA353 | |
| J | LEU274 | |
| A | ALA353 | |
| J | ALA353 | |
| K | LEU274 | |
| K | ALA353 | |
| L | LEU274 | |
| L | ALA353 | |
| B | LEU274 | |
| B | ALA353 | |
| C | LEU274 | |
| C | ALA353 | |
| D | LEU274 | |
| D | ALA353 | |
| E | LEU274 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8099447, ECO:0000305|PubMed:11329256, ECO:0007744|PDB:1FPY, ECO:0007744|PDB:2LGS |
| Chain | Residue | Details |
| A | LEU322 | |
| J | LEU322 | |
| K | LEU322 | |
| L | LEU322 | |
| B | LEU322 | |
| C | LEU322 | |
| D | LEU322 | |
| E | LEU322 | |
| F | LEU322 | |
| G | LEU322 | |
| H | LEU322 | |
| I | LEU322 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:11329256, ECO:0007744|PDB:1FPY |
| Chain | Residue | Details |
| A | ALA328 | |
| J | ALA328 | |
| K | ALA328 | |
| L | ALA328 | |
| B | ALA328 | |
| C | ALA328 | |
| D | ALA328 | |
| E | ALA328 | |
| F | ALA328 | |
| G | ALA328 | |
| H | ALA328 | |
| I | ALA328 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P9WN39 |
| Chain | Residue | Details |
| A | SER340 | |
| E | ILE345 | |
| F | SER340 | |
| F | ILE345 | |
| G | SER340 | |
| G | ILE345 | |
| H | SER340 | |
| H | ILE345 | |
| I | SER340 | |
| I | ILE345 | |
| J | SER340 | |
| A | ILE345 | |
| J | ILE345 | |
| K | SER340 | |
| K | ILE345 | |
| L | SER340 | |
| L | ILE345 | |
| B | SER340 | |
| B | ILE345 | |
| C | SER340 | |
| C | ILE345 | |
| D | SER340 | |
| D | ILE345 | |
| E | SER340 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11329256, ECO:0000269|PubMed:2572586, ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447, ECO:0007744|PDB:1F1H, ECO:0007744|PDB:1F52, ECO:0007744|PDB:1FPY, ECO:0007744|PDB:1LGR, ECO:0007744|PDB:2GLS, ECO:0007744|PDB:2LGS |
| Chain | Residue | Details |
| A | VAL358 | |
| J | VAL358 | |
| K | VAL358 | |
| L | VAL358 | |
| B | VAL358 | |
| C | VAL358 | |
| D | VAL358 | |
| E | VAL358 | |
| F | VAL358 | |
| G | VAL358 | |
| H | VAL358 | |
| I | VAL358 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8099447, ECO:0007744|PDB:2LGS |
| Chain | Residue | Details |
| A | PHE360 | |
| J | PHE360 | |
| K | PHE360 | |
| L | PHE360 | |
| B | PHE360 | |
| C | PHE360 | |
| D | PHE360 | |
| E | PHE360 | |
| F | PHE360 | |
| G | PHE360 | |
| H | PHE360 | |
| I | PHE360 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 12 |
| Details | MOD_RES: O-AMP-tyrosine => ECO:0000250|UniProtKB:P9WN39 |
| Chain | Residue | Details |
| A | ASP398 | |
| J | ASP398 | |
| K | ASP398 | |
| L | ASP398 | |
| B | ASP398 | |
| C | ASP398 | |
| D | ASP398 | |
| E | ASP398 | |
| F | ASP398 | |
| G | ASP398 | |
| H | ASP398 | |
| I | ASP398 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| A | ARG339 | |
| A | ASP50 | |
| A | GLU327 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| J | ARG339 | |
| J | ASP50 | |
| J | GLU327 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| K | ARG339 | |
| K | ASP50 | |
| K | GLU327 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| L | ARG339 | |
| L | ASP50 | |
| L | GLU327 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| B | ARG339 | |
| B | ASP50 | |
| B | GLU327 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| C | ARG339 | |
| C | ASP50 | |
| C | GLU327 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| D | ARG339 | |
| D | ASP50 | |
| D | GLU327 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| E | ARG339 | |
| E | ASP50 | |
| E | GLU327 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| F | ARG339 | |
| F | ASP50 | |
| F | GLU327 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| G | ARG339 | |
| G | ASP50 | |
| G | GLU327 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| H | ARG339 | |
| H | ASP50 | |
| H | GLU327 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| I | ARG339 | |
| I | ASP50 | |
| I | GLU327 |
