2WHI
Crystal structure of Mycobacterium Tuberculosis Glutamine Synthetase in complex with a purine analogue inhibitor and L-methionine-S- sulfoximine phosphate.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0001968 | molecular_function | fibronectin binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004356 | molecular_function | glutamine synthetase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006542 | biological_process | glutamine biosynthetic process |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| A | 0010756 | biological_process | positive regulation of plasminogen activation |
| A | 0016020 | cellular_component | membrane |
| A | 0016874 | molecular_function | ligase activity |
| A | 0019740 | biological_process | nitrogen utilization |
| A | 0035375 | molecular_function | zymogen binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051260 | biological_process | protein homooligomerization |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0001968 | molecular_function | fibronectin binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004356 | molecular_function | glutamine synthetase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006542 | biological_process | glutamine biosynthetic process |
| B | 0009274 | cellular_component | peptidoglycan-based cell wall |
| B | 0010756 | biological_process | positive regulation of plasminogen activation |
| B | 0016020 | cellular_component | membrane |
| B | 0016874 | molecular_function | ligase activity |
| B | 0019740 | biological_process | nitrogen utilization |
| B | 0035375 | molecular_function | zymogen binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051260 | biological_process | protein homooligomerization |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0001968 | molecular_function | fibronectin binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004356 | molecular_function | glutamine synthetase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006542 | biological_process | glutamine biosynthetic process |
| C | 0009274 | cellular_component | peptidoglycan-based cell wall |
| C | 0010756 | biological_process | positive regulation of plasminogen activation |
| C | 0016020 | cellular_component | membrane |
| C | 0016874 | molecular_function | ligase activity |
| C | 0019740 | biological_process | nitrogen utilization |
| C | 0035375 | molecular_function | zymogen binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051260 | biological_process | protein homooligomerization |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0001968 | molecular_function | fibronectin binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004356 | molecular_function | glutamine synthetase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006542 | biological_process | glutamine biosynthetic process |
| D | 0009274 | cellular_component | peptidoglycan-based cell wall |
| D | 0010756 | biological_process | positive regulation of plasminogen activation |
| D | 0016020 | cellular_component | membrane |
| D | 0016874 | molecular_function | ligase activity |
| D | 0019740 | biological_process | nitrogen utilization |
| D | 0035375 | molecular_function | zymogen binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051260 | biological_process | protein homooligomerization |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0001968 | molecular_function | fibronectin binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004356 | molecular_function | glutamine synthetase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005576 | cellular_component | extracellular region |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0006542 | biological_process | glutamine biosynthetic process |
| E | 0009274 | cellular_component | peptidoglycan-based cell wall |
| E | 0010756 | biological_process | positive regulation of plasminogen activation |
| E | 0016020 | cellular_component | membrane |
| E | 0016874 | molecular_function | ligase activity |
| E | 0019740 | biological_process | nitrogen utilization |
| E | 0035375 | molecular_function | zymogen binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051260 | biological_process | protein homooligomerization |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0001968 | molecular_function | fibronectin binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004356 | molecular_function | glutamine synthetase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005576 | cellular_component | extracellular region |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0006542 | biological_process | glutamine biosynthetic process |
| F | 0009274 | cellular_component | peptidoglycan-based cell wall |
| F | 0010756 | biological_process | positive regulation of plasminogen activation |
| F | 0016020 | cellular_component | membrane |
| F | 0016874 | molecular_function | ligase activity |
| F | 0019740 | biological_process | nitrogen utilization |
| F | 0035375 | molecular_function | zymogen binding |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051260 | biological_process | protein homooligomerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 1AZ A 501 |
| Chain | Residue |
| A | TYR129 |
| A | PO4506 |
| A | HOH2153 |
| A | GLY131 |
| A | TYR230 |
| A | PHE232 |
| A | HIS278 |
| A | SER280 |
| A | TRP282 |
| A | LYS361 |
| A | ARG364 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 502 |
| Chain | Residue |
| A | GLU135 |
| A | GLU219 |
| A | GLU227 |
| A | P3S505 |
| A | HOH2159 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 503 |
| Chain | Residue |
| A | GLU133 |
| A | HIS276 |
| A | GLU366 |
| A | P3S505 |
| A | PO4506 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 504 |
| Chain | Residue |
| A | GLU133 |
| A | GLU227 |
| A | P3S505 |
| A | PO4506 |
| A | HOH2156 |
| A | HOH2161 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE P3S A 505 |
| Chain | Residue |
| A | GLU133 |
| A | GLU135 |
| A | GLU219 |
| A | GLU227 |
| A | GLY272 |
| A | HIS276 |
| A | ARG329 |
| A | GLU335 |
| A | ARG347 |
| A | GLU366 |
| A | ARG368 |
| A | MG502 |
| A | MG503 |
| A | MG504 |
| A | PO4506 |
| A | HOH2125 |
| A | HOH2156 |
| A | HOH2157 |
| A | HOH2159 |
| A | HOH2273 |
| F | ASP54 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 506 |
| Chain | Residue |
| A | GLU133 |
| A | HIS278 |
| A | ARG347 |
| A | ARG352 |
| A | GLU366 |
| A | 1AZ501 |
| A | MG503 |
| A | MG504 |
| A | P3S505 |
| A | HOH2161 |
| A | HOH2274 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 507 |
| Chain | Residue |
| A | SER424 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 1PE A 508 |
| Chain | Residue |
| A | SER56 |
| A | SER57 |
| A | ARG59 |
| A | HOH2276 |
| B | LYS183 |
| B | HOH2118 |
| E | LEU474 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 1AZ B 501 |
| Chain | Residue |
| B | TYR129 |
| B | GLY131 |
| B | TYR230 |
| B | PHE232 |
| B | HIS278 |
| B | SER280 |
| B | TRP282 |
| B | LYS361 |
| B | ARG364 |
| B | PO4506 |
| B | HOH2152 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 502 |
| Chain | Residue |
| B | GLU135 |
| B | GLU219 |
| B | GLU227 |
| B | P3S505 |
| B | HOH2274 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 503 |
| Chain | Residue |
| B | GLU133 |
| B | HIS276 |
| B | GLU366 |
| B | P3S505 |
| B | PO4506 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 504 |
| Chain | Residue |
| B | GLU133 |
| B | GLU227 |
| B | P3S505 |
| B | PO4506 |
| B | HOH2155 |
| B | HOH2160 |
| site_id | BC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE P3S B 505 |
| Chain | Residue |
| B | GLY272 |
| B | HIS276 |
| B | ARG329 |
| B | GLU335 |
| B | ARG347 |
| B | GLU366 |
| B | ARG368 |
| B | MG502 |
| B | MG503 |
| B | MG504 |
| B | PO4506 |
| B | HOH2123 |
| B | HOH2157 |
| B | HOH2273 |
| B | HOH2274 |
| A | ASP54 |
| B | GLU133 |
| B | GLU135 |
| B | GLU219 |
| B | GLU227 |
| site_id | BC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PO4 B 506 |
| Chain | Residue |
| B | GLU133 |
| B | HIS278 |
| B | ARG347 |
| B | ARG352 |
| B | GLU366 |
| B | 1AZ501 |
| B | MG503 |
| B | MG504 |
| B | P3S505 |
| B | HOH2160 |
| B | HOH2275 |
| B | HOH2276 |
| site_id | BC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 507 |
| Chain | Residue |
| B | SER424 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 1PE B 508 |
| Chain | Residue |
| B | SER56 |
| B | SER57 |
| B | ARG59 |
| B | PHE454 |
| B | HOH2277 |
| C | LYS183 |
| C | HOH2116 |
| D | LEU474 |
| site_id | BC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 1AZ C 501 |
| Chain | Residue |
| C | TYR129 |
| C | GLY131 |
| C | TYR230 |
| C | PHE232 |
| C | HIS278 |
| C | SER280 |
| C | TRP282 |
| C | LYS361 |
| C | ARG364 |
| C | PO4506 |
| C | HOH2151 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 502 |
| Chain | Residue |
| C | GLU135 |
| C | GLU219 |
| C | GLU227 |
| C | P3S505 |
| C | HOH2157 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 503 |
| Chain | Residue |
| C | GLU133 |
| C | HIS276 |
| C | GLU366 |
| C | ARG368 |
| C | P3S505 |
| C | PO4506 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 504 |
| Chain | Residue |
| C | GLU133 |
| C | GLU227 |
| C | P3S505 |
| C | PO4506 |
| C | HOH2154 |
| C | HOH2159 |
| site_id | CC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE P3S C 505 |
| Chain | Residue |
| B | ASP54 |
| C | GLU133 |
| C | GLU135 |
| C | GLU219 |
| C | GLU227 |
| C | GLY272 |
| C | HIS276 |
| C | ARG329 |
| C | GLU335 |
| C | ARG347 |
| C | GLU366 |
| C | ARG368 |
| C | MG502 |
| C | MG503 |
| C | MG504 |
| C | PO4506 |
| C | HOH2121 |
| C | HOH2154 |
| C | HOH2155 |
| C | HOH2157 |
| C | HOH2271 |
| site_id | CC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PO4 C 506 |
| Chain | Residue |
| C | GLU133 |
| C | HIS278 |
| C | ARG347 |
| C | ARG352 |
| C | GLU366 |
| C | 1AZ501 |
| C | MG503 |
| C | MG504 |
| C | P3S505 |
| C | HOH2154 |
| C | HOH2159 |
| C | HOH2273 |
| site_id | CC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL C 507 |
| Chain | Residue |
| C | SER424 |
| site_id | CC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 1PE C 508 |
| Chain | Residue |
| C | SER56 |
| C | SER57 |
| C | ARG59 |
| C | PHE454 |
| C | GLU459 |
| C | LEU474 |
| C | HOH2274 |
| D | LYS183 |
| site_id | CC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 1AZ D 501 |
| Chain | Residue |
| D | TYR129 |
| D | GLY131 |
| D | TYR230 |
| D | PHE232 |
| D | HIS278 |
| D | SER280 |
| D | TRP282 |
| D | LYS361 |
| D | ARG364 |
| D | PO4506 |
| D | HOH2151 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 502 |
| Chain | Residue |
| D | GLU135 |
| D | GLU219 |
| D | GLU227 |
| D | P3S505 |
| D | HOH2275 |
| site_id | CC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 503 |
| Chain | Residue |
| D | GLU133 |
| D | HIS276 |
| D | GLU366 |
| D | P3S505 |
| D | PO4506 |
| site_id | DC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 504 |
| Chain | Residue |
| D | GLU133 |
| D | GLU227 |
| D | P3S505 |
| D | PO4506 |
| D | HOH2154 |
| D | HOH2159 |
| site_id | DC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE P3S D 505 |
| Chain | Residue |
| C | ASP54 |
| D | GLU133 |
| D | GLU135 |
| D | GLU219 |
| D | GLU227 |
| D | GLY272 |
| D | HIS276 |
| D | ARG329 |
| D | GLU335 |
| D | ARG347 |
| D | GLU366 |
| D | ARG368 |
| D | MG502 |
| D | MG503 |
| D | MG504 |
| D | PO4506 |
| D | HOH2123 |
| D | HOH2156 |
| D | HOH2275 |
| D | HOH2276 |
| site_id | DC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 D 506 |
| Chain | Residue |
| D | GLU133 |
| D | HIS278 |
| D | ARG347 |
| D | ARG352 |
| D | GLU366 |
| D | 1AZ501 |
| D | MG503 |
| D | MG504 |
| D | P3S505 |
| D | HOH2159 |
| D | HOH2278 |
| site_id | DC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL D 507 |
| Chain | Residue |
| D | SER424 |
| site_id | DC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1PE D 508 |
| Chain | Residue |
| B | LEU474 |
| D | SER56 |
| D | SER57 |
| D | ARG59 |
| D | HOH2279 |
| E | LYS183 |
| site_id | DC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 1AZ E 501 |
| Chain | Residue |
| E | TYR129 |
| E | GLY131 |
| E | TYR230 |
| E | PHE232 |
| E | HIS278 |
| E | SER280 |
| E | TRP282 |
| E | LYS361 |
| E | ARG364 |
| E | PO4506 |
| E | HOH2150 |
| site_id | DC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG E 502 |
| Chain | Residue |
| E | GLU135 |
| E | GLU219 |
| E | GLU227 |
| E | P3S505 |
| E | HOH2271 |
| site_id | DC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG E 503 |
| Chain | Residue |
| E | GLU133 |
| E | HIS276 |
| E | GLU366 |
| E | P3S505 |
| E | PO4506 |
| site_id | DC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG E 504 |
| Chain | Residue |
| E | GLU133 |
| E | GLU227 |
| E | P3S505 |
| E | PO4506 |
| E | HOH2152 |
| E | HOH2156 |
| site_id | EC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE P3S E 505 |
| Chain | Residue |
| D | ASP54 |
| E | GLU133 |
| E | GLU135 |
| E | GLU219 |
| E | GLU227 |
| E | GLY272 |
| E | HIS276 |
| E | ARG329 |
| E | GLU335 |
| E | ARG347 |
| E | GLU366 |
| E | ARG368 |
| E | MG502 |
| E | MG503 |
| E | MG504 |
| E | PO4506 |
| E | HOH2121 |
| E | HOH2152 |
| E | HOH2153 |
| E | HOH2271 |
| E | HOH2272 |
| site_id | EC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 E 506 |
| Chain | Residue |
| E | GLU133 |
| E | HIS278 |
| E | ARG347 |
| E | ARG352 |
| E | GLU366 |
| E | 1AZ501 |
| E | MG503 |
| E | MG504 |
| E | P3S505 |
| E | HOH2156 |
| E | HOH2274 |
| site_id | EC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL E 507 |
| Chain | Residue |
| E | SER424 |
| site_id | EC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1PE E 508 |
| Chain | Residue |
| A | LEU474 |
| E | SER56 |
| E | SER57 |
| E | ARG59 |
| E | HOH2275 |
| F | LYS183 |
| site_id | EC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 1AZ F 501 |
| Chain | Residue |
| F | TYR129 |
| F | GLY131 |
| F | TYR230 |
| F | PHE232 |
| F | HIS278 |
| F | SER280 |
| F | TRP282 |
| F | LYS361 |
| F | ARG364 |
| F | PO4506 |
| F | HOH2148 |
| site_id | EC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG F 502 |
| Chain | Residue |
| F | GLU135 |
| F | GLU219 |
| F | GLU227 |
| F | P3S505 |
| F | HOH2067 |
| site_id | EC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG F 503 |
| Chain | Residue |
| F | GLU133 |
| F | HIS276 |
| F | GLU366 |
| F | P3S505 |
| F | PO4506 |
| site_id | EC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 504 |
| Chain | Residue |
| F | GLU133 |
| F | GLU227 |
| F | P3S505 |
| F | PO4506 |
| F | HOH2150 |
| F | HOH2154 |
| site_id | EC9 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE P3S F 505 |
| Chain | Residue |
| E | ASP54 |
| F | GLU133 |
| F | GLU135 |
| F | GLU219 |
| F | GLU227 |
| F | GLY272 |
| F | HIS276 |
| F | ARG329 |
| F | GLU335 |
| F | ARG347 |
| F | GLU366 |
| F | ARG368 |
| F | MG502 |
| F | MG503 |
| F | MG504 |
| F | PO4506 |
| F | HOH2067 |
| F | HOH2121 |
| F | HOH2150 |
| F | HOH2151 |
| F | HOH2266 |
| site_id | FC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PO4 F 506 |
| Chain | Residue |
| F | GLU133 |
| F | HIS278 |
| F | ARG347 |
| F | ARG352 |
| F | GLU366 |
| F | 1AZ501 |
| F | MG503 |
| F | MG504 |
| F | P3S505 |
| F | HOH2154 |
| F | HOH2267 |
| F | HOH2268 |
| site_id | FC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL F 507 |
| Chain | Residue |
| F | SER424 |
| site_id | FC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1PE F 508 |
| Chain | Residue |
| A | LYS183 |
| F | SER57 |
| F | ARG59 |
| F | GLU459 |
| F | LEU474 |
| F | HOH2269 |
Functional Information from PROSITE/UniProt
| site_id | PS00180 |
| Number of Residues | 19 |
| Details | GLNA_1 Glutamine synthetase signature 1. FDGSSirgfqsihESDmlL |
| Chain | Residue | Details |
| A | PHE53-LEU71 |
| site_id | PS00181 |
| Number of Residues | 16 |
| Details | GLNA_ATP Glutamine synthetase putative ATP-binding region signature. KPLfgd..NGSGmHchqS |
| Chain | Residue | Details |
| A | LYS265-SER280 |
| site_id | PS00182 |
| Number of Residues | 13 |
| Details | GLNA_ADENYLATION Glutamine synthetase class-I adenylation site. KIepqapVDKDLY |
| Chain | Residue | Details |
| A | LYS394-TYR406 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 504 |
| Details | Domain: {"description":"GS beta-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU01330","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2220 |
| Details | Domain: {"description":"GS catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU01331","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16027359","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19695264","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22369127","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2012","firstPage":"620","lastPage":"626","volume":"3","journal":"Med. Chem. Commun.","title":"Synthesis, biological evaluation and X-Ray crystallographic studies of imidazo(1,2-A)pyridine-based Mycobacterium tuberculosis glutamine synthetase inhibitors.","authors":["Nordqvist A.","Nilsson M.T.","Lagerlund O.","Muthas D.","Gising J.","Yahiaoui S.","Odell L.R.","Srinivasa B.R.","Larhed M.","Mowbray S.L.","Karlen A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/C2MD00310D"}]}},{"source":"PDB","id":"2BVC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WHI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZXR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZXV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ACF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16027359","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2BVC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16027359","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19695264","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22369127","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"journal article","publicationDate":"2012","firstPage":"620","lastPage":"626","volume":"3","journal":"Med. Chem. Commun.","title":"Synthesis, biological evaluation and X-Ray crystallographic studies of imidazo(1,2-A)pyridine-based Mycobacterium tuberculosis glutamine synthetase inhibitors.","authors":["Nordqvist A.","Nilsson M.T.","Lagerlund O.","Muthas D.","Gising J.","Yahiaoui S.","Odell L.R.","Srinivasa B.R.","Larhed M.","Mowbray S.L.","Karlen A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/C2MD00310D"}]}},{"source":"PDB","id":"2BVC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WHI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZXR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZXV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ACF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P12425","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P77961","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A1P6","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16027359","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22369127","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"journal article","publicationDate":"2012","firstPage":"620","lastPage":"626","volume":"3","journal":"Med. Chem. Commun.","title":"Synthesis, biological evaluation and X-Ray crystallographic studies of imidazo(1,2-A)pyridine-based Mycobacterium tuberculosis glutamine synthetase inhibitors.","authors":["Nordqvist A.","Nilsson M.T.","Lagerlund O.","Muthas D.","Gising J.","Yahiaoui S.","Odell L.R.","Srinivasa B.R.","Larhed M.","Mowbray S.L.","Karlen A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/C2MD00310D"}]}},{"source":"PDB","id":"2BVC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZXR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZXV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ACF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"O-AMP-tyrosine","evidences":[{"source":"PubMed","id":"15037612","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12146952","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16027359","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| A | ASP54 | |
| A | ARG347 | |
| A | GLU335 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| B | ASP54 | |
| B | ARG347 | |
| B | GLU335 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| C | ASP54 | |
| C | ARG347 | |
| C | GLU335 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| D | ASP54 | |
| D | ARG347 | |
| D | GLU335 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| E | ASP54 | |
| E | ARG347 | |
| E | GLU335 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| F | ASP54 | |
| F | ARG347 | |
| F | GLU335 |
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 537 |
| Chain | Residue | Details |
| A | ASP54 | activator, proton acceptor |
| A | GLU133 | metal ligand |
| A | GLU135 | metal ligand |
| A | GLU219 | metal ligand |
| A | GLU227 | metal ligand |
| A | HIS276 | metal ligand |
| A | ARG347 | electrostatic stabiliser |
| A | GLU366 | metal ligand |
| A | ARG368 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 537 |
| Chain | Residue | Details |
| B | ASP54 | activator, proton acceptor |
| B | GLU133 | metal ligand |
| B | GLU135 | metal ligand |
| B | GLU219 | metal ligand |
| B | GLU227 | metal ligand |
| B | HIS276 | metal ligand |
| B | ARG347 | electrostatic stabiliser |
| B | GLU366 | metal ligand |
| B | ARG368 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 9 |
| Details | M-CSA 537 |
| Chain | Residue | Details |
| C | ASP54 | activator, proton acceptor |
| C | GLU133 | metal ligand |
| C | GLU135 | metal ligand |
| C | GLU219 | metal ligand |
| C | GLU227 | metal ligand |
| C | HIS276 | metal ligand |
| C | ARG347 | electrostatic stabiliser |
| C | GLU366 | metal ligand |
| C | ARG368 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 9 |
| Details | M-CSA 537 |
| Chain | Residue | Details |
| D | ASP54 | activator, proton acceptor |
| D | GLU133 | metal ligand |
| D | GLU135 | metal ligand |
| D | GLU219 | metal ligand |
| D | GLU227 | metal ligand |
| D | HIS276 | metal ligand |
| D | ARG347 | electrostatic stabiliser |
| D | GLU366 | metal ligand |
| D | ARG368 | electrostatic stabiliser |
| site_id | MCSA5 |
| Number of Residues | 9 |
| Details | M-CSA 537 |
| Chain | Residue | Details |
| E | ASP54 | activator, proton acceptor |
| E | GLU133 | metal ligand |
| E | GLU135 | metal ligand |
| E | GLU219 | metal ligand |
| E | GLU227 | metal ligand |
| E | HIS276 | metal ligand |
| E | ARG347 | electrostatic stabiliser |
| E | GLU366 | metal ligand |
| E | ARG368 | electrostatic stabiliser |
| site_id | MCSA6 |
| Number of Residues | 9 |
| Details | M-CSA 537 |
| Chain | Residue | Details |
| F | ASP54 | activator, proton acceptor |
| F | GLU133 | metal ligand |
| F | GLU135 | metal ligand |
| F | GLU219 | metal ligand |
| F | GLU227 | metal ligand |
| F | HIS276 | metal ligand |
| F | ARG347 | electrostatic stabiliser |
| F | GLU366 | metal ligand |
| F | ARG368 | electrostatic stabiliser |
