4ACF
CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS GLUTAMINE SYNTHETASE IN COMPLEX WITH IMIDAZOPYRIDINE INHIBITOR ((4-(6-BROMO-3-(BUTYLAMINO)IMIDAZO(1,2-A)PYRIDIN-2-YL)PHENOXY) ACETIC ACID) AND L-METHIONINE-S-SULFOXIMINE PHOSPHATE.
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 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 | 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 | 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 | 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 | 8 |
Details | BINDING SITE FOR RESIDUE 46B A 1479 |
Chain | Residue |
A | TYR129 |
A | PHE232 |
A | HIS278 |
A | TRP282 |
A | ASN359 |
A | LYS361 |
A | ARG364 |
A | HOH2248 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 1480 |
Chain | Residue |
A | GLU219 |
A | GLU227 |
A | P3S1483 |
A | HOH2123 |
A | GLU135 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 1481 |
Chain | Residue |
A | GLU133 |
A | HIS276 |
A | GLU366 |
A | ARG368 |
A | P3S1483 |
A | PO41484 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG A 1482 |
Chain | Residue |
A | GLU133 |
A | GLU227 |
A | ASN229 |
A | P3S1483 |
A | PO41484 |
A | HOH2124 |
A | HOH2217 |
site_id | AC5 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE P3S A 1483 |
Chain | Residue |
A | GLU133 |
A | GLU135 |
A | GLU219 |
A | GLU227 |
A | GLY272 |
A | GLY274 |
A | HIS276 |
A | ARG329 |
A | GLU335 |
A | ARG347 |
A | GLU366 |
A | ARG368 |
A | MG1480 |
A | MG1481 |
A | MG1482 |
A | PO41484 |
A | HOH2123 |
A | HOH2182 |
A | HOH2217 |
A | HOH2220 |
A | HOH2246 |
F | ASP54 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PO4 A 1484 |
Chain | Residue |
A | GLU133 |
A | HIS278 |
A | ARG347 |
A | ARG352 |
A | GLU366 |
A | MG1481 |
A | MG1482 |
A | P3S1483 |
A | HOH2124 |
A | HOH2217 |
A | HOH2218 |
A | HOH2300 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 1485 |
Chain | Residue |
A | SER424 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 1486 |
Chain | Residue |
A | HIS237 |
A | HOH2067 |
A | HOH2068 |
A | HOH2224 |
A | HOH2225 |
A | HOH2349 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 46B B 1479 |
Chain | Residue |
B | TYR129 |
B | GLY131 |
B | PHE232 |
B | HIS278 |
B | TRP282 |
B | ASN359 |
B | LYS361 |
B | ARG364 |
B | HOH2229 |
E | LYS14 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 1480 |
Chain | Residue |
B | GLU135 |
B | GLU219 |
B | GLU227 |
B | P3S1483 |
B | HOH2122 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 1481 |
Chain | Residue |
B | GLU133 |
B | HIS276 |
B | GLU366 |
B | P3S1483 |
B | PO41484 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 1482 |
Chain | Residue |
B | GLU133 |
B | GLU227 |
B | P3S1483 |
B | PO41484 |
B | HOH2121 |
B | HOH2200 |
site_id | BC4 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE P3S B 1483 |
Chain | Residue |
B | HIS276 |
B | ARG329 |
B | GLU335 |
B | ARG347 |
B | GLU366 |
B | ARG368 |
B | MG1480 |
B | MG1481 |
B | MG1482 |
B | PO41484 |
B | HOH2122 |
B | HOH2174 |
B | HOH2200 |
B | HOH2201 |
B | HOH2227 |
A | ASP54 |
B | GLU133 |
B | GLU135 |
B | GLU219 |
B | GLU227 |
B | GLY272 |
site_id | BC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PO4 B 1484 |
Chain | Residue |
B | GLU133 |
B | HIS278 |
B | ARG347 |
B | ARG352 |
B | GLU366 |
B | MG1481 |
B | MG1482 |
B | P3S1483 |
B | HOH2121 |
B | HOH2199 |
B | HOH2200 |
B | HOH2277 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 1485 |
Chain | Residue |
B | SER424 |
B | HOH2320 |
site_id | BC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG B 1486 |
Chain | Residue |
B | GLU76 |
B | HIS237 |
B | HOH2065 |
B | HOH2066 |
B | HOH2205 |
B | HOH2206 |
B | HOH2325 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 46B C 1479 |
Chain | Residue |
C | TYR129 |
C | PHE232 |
C | HIS278 |
C | TRP282 |
C | ASN359 |
C | LYS361 |
C | ARG364 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 1480 |
Chain | Residue |
C | GLU135 |
C | GLU219 |
C | GLU227 |
C | P3S1483 |
C | HOH2119 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 1481 |
Chain | Residue |
C | GLU133 |
C | HIS276 |
C | GLU366 |
C | ARG368 |
C | P3S1483 |
C | PO41484 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 1482 |
Chain | Residue |
C | GLU133 |
C | GLU227 |
C | P3S1483 |
C | PO41484 |
C | HOH2118 |
C | HOH2195 |
site_id | CC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE P3S C 1483 |
Chain | Residue |
B | ASP54 |
C | GLU133 |
C | GLU135 |
C | GLU219 |
C | GLU227 |
C | GLY272 |
C | HIS276 |
C | ARG329 |
C | TYR334 |
C | GLU335 |
C | ARG347 |
C | GLU366 |
C | ARG368 |
C | MG1480 |
C | MG1481 |
C | MG1482 |
C | PO41484 |
C | HOH2119 |
C | HOH2171 |
C | HOH2195 |
C | HOH2196 |
C | HOH2223 |
site_id | CC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PO4 C 1484 |
Chain | Residue |
C | GLU133 |
C | HIS278 |
C | ARG347 |
C | ARG352 |
C | GLU366 |
C | MG1481 |
C | MG1482 |
C | P3S1483 |
C | HOH2118 |
C | HOH2194 |
C | HOH2195 |
C | HOH2273 |
site_id | CC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL C 1485 |
Chain | Residue |
C | LEU423 |
C | SER424 |
site_id | CC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG C 1486 |
Chain | Residue |
C | GLU76 |
C | HIS237 |
C | HOH2064 |
C | HOH2065 |
C | HOH2200 |
C | HOH2201 |
C | HOH2320 |
site_id | CC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 46B D 1479 |
Chain | Residue |
D | TYR129 |
D | PHE232 |
D | HIS278 |
D | TRP282 |
D | ASN359 |
D | LYS361 |
D | ARG364 |
D | HOH2223 |
site_id | CC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 1480 |
Chain | Residue |
D | GLU135 |
D | GLU219 |
D | GLU227 |
D | MG1482 |
D | P3S1483 |
D | HOH2114 |
site_id | CC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 1481 |
Chain | Residue |
D | GLU133 |
D | HIS276 |
D | GLU366 |
D | ARG368 |
D | P3S1483 |
D | PO41484 |
site_id | DC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG D 1482 |
Chain | Residue |
D | GLU133 |
D | GLU227 |
D | MG1480 |
D | P3S1483 |
D | PO41484 |
D | HOH2115 |
D | HOH2193 |
site_id | DC2 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE P3S D 1483 |
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 | MG1480 |
D | MG1481 |
D | MG1482 |
D | PO41484 |
D | HOH2114 |
D | HOH2167 |
D | HOH2193 |
D | HOH2194 |
D | HOH2222 |
site_id | DC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PO4 D 1484 |
Chain | Residue |
D | GLU133 |
D | HIS278 |
D | ARG347 |
D | ARG352 |
D | GLU366 |
D | MG1481 |
D | MG1482 |
D | P3S1483 |
D | HOH2115 |
D | HOH2193 |
D | HOH2270 |
site_id | DC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL D 1485 |
Chain | Residue |
D | SER424 |
site_id | DC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG D 1486 |
Chain | Residue |
D | GLU76 |
D | HIS237 |
D | HOH2061 |
D | HOH2062 |
D | HOH2198 |
D | HOH2199 |
D | HOH2318 |
site_id | DC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 46B E 1479 |
Chain | Residue |
E | TYR129 |
E | PHE232 |
E | HIS278 |
E | TRP282 |
E | ASN359 |
E | LYS361 |
E | ARG364 |
E | HOH2224 |
site_id | DC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG E 1480 |
Chain | Residue |
E | GLU135 |
E | GLU219 |
E | GLU227 |
E | MG1482 |
E | P3S1483 |
E | HOH2116 |
site_id | DC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG E 1481 |
Chain | Residue |
E | GLU133 |
E | HIS276 |
E | GLU366 |
E | ARG368 |
E | P3S1483 |
E | PO41484 |
site_id | DC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG E 1482 |
Chain | Residue |
E | GLU133 |
E | GLU227 |
E | MG1480 |
E | P3S1483 |
E | PO41484 |
E | HOH2115 |
E | HOH2194 |
site_id | EC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE P3S E 1483 |
Chain | Residue |
D | ASP54 |
E | GLU133 |
E | GLU135 |
E | GLU219 |
E | GLU227 |
E | GLY272 |
E | HIS276 |
E | ARG329 |
E | TYR334 |
E | GLU335 |
E | ARG347 |
E | GLU366 |
E | ARG368 |
E | MG1480 |
E | MG1481 |
E | MG1482 |
E | PO41484 |
E | HOH2116 |
E | HOH2169 |
E | HOH2194 |
E | HOH2196 |
E | HOH2222 |
site_id | EC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PO4 E 1484 |
Chain | Residue |
E | GLU133 |
E | HIS278 |
E | ARG347 |
E | ARG352 |
E | GLU366 |
E | MG1481 |
E | MG1482 |
E | P3S1483 |
E | HOH2115 |
E | HOH2194 |
E | HOH2195 |
E | HOH2272 |
site_id | EC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL E 1485 |
Chain | Residue |
E | SER424 |
site_id | EC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG E 1486 |
Chain | Residue |
E | GLU76 |
E | HIS237 |
E | HOH2064 |
E | HOH2065 |
E | HOH2200 |
E | HOH2201 |
E | HOH2320 |
site_id | EC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 46B F 1479 |
Chain | Residue |
F | TYR129 |
F | PHE232 |
F | HIS278 |
F | TRP282 |
F | ASN359 |
F | LYS361 |
F | ARG364 |
F | HOH2199 |
site_id | EC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG F 1480 |
Chain | Residue |
F | GLU135 |
F | GLU219 |
F | GLU227 |
F | MG1482 |
F | P3S1483 |
F | HOH2095 |
site_id | EC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG F 1481 |
Chain | Residue |
F | GLU133 |
F | HIS276 |
F | GLU366 |
F | P3S1483 |
F | PO41484 |
site_id | EC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG F 1482 |
Chain | Residue |
F | GLU133 |
F | GLU227 |
F | MG1480 |
F | P3S1483 |
F | PO41484 |
F | HOH2096 |
F | HOH2171 |
site_id | EC9 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE P3S F 1483 |
Chain | Residue |
E | ASP54 |
F | GLU133 |
F | GLU135 |
F | GLU219 |
F | GLU227 |
F | GLY272 |
F | GLY274 |
F | HIS276 |
F | ARG329 |
F | GLU335 |
F | ALA336 |
F | ARG347 |
F | GLU366 |
F | ARG368 |
F | MG1480 |
F | MG1481 |
F | MG1482 |
F | PO41484 |
F | HOH2095 |
F | HOH2147 |
F | HOH2171 |
F | HOH2173 |
F | HOH2197 |
site_id | FC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PO4 F 1484 |
Chain | Residue |
F | GLU133 |
F | HIS278 |
F | ARG347 |
F | ARG352 |
F | GLU366 |
F | MG1481 |
F | MG1482 |
F | P3S1483 |
F | HOH2096 |
F | HOH2171 |
F | HOH2172 |
F | HOH2247 |
site_id | FC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL F 1485 |
Chain | Residue |
F | SER424 |
site_id | FC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG F 1486 |
Chain | Residue |
F | HIS237 |
F | HOH2046 |
F | HOH2047 |
F | HOH2177 |
F | HOH2178 |
F | HOH2294 |
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 | 36 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16027359, ECO:0000269|PubMed:19695264, ECO:0000269|PubMed:22369127, ECO:0000269|DOI:10.1039/C2MD00310D, ECO:0007744|PDB:2BVC, ECO:0007744|PDB:2WHI, ECO:0007744|PDB:3ZXR, ECO:0007744|PDB:3ZXV, ECO:0007744|PDB:4ACF |
Chain | Residue | Details |
A | GLU133 | |
B | GLU227 | |
B | HIS276 | |
B | GLU366 | |
C | GLU133 | |
C | GLU135 | |
C | GLU219 | |
C | GLU227 | |
C | HIS276 | |
C | GLU366 | |
D | GLU133 | |
A | GLU135 | |
D | GLU135 | |
D | GLU219 | |
D | GLU227 | |
D | HIS276 | |
D | GLU366 | |
E | GLU133 | |
E | GLU135 | |
E | GLU219 | |
E | GLU227 | |
E | HIS276 | |
A | GLU219 | |
E | GLU366 | |
F | GLU133 | |
F | GLU135 | |
F | GLU219 | |
F | GLU227 | |
F | HIS276 | |
F | GLU366 | |
A | GLU227 | |
A | HIS276 | |
A | GLU366 | |
B | GLU133 | |
B | GLU135 | |
B | GLU219 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000305|PubMed:16027359, ECO:0007744|PDB:2BVC |
Chain | Residue | Details |
A | GLU214 | |
E | TYR230 | |
F | GLU214 | |
F | TYR230 | |
A | TYR230 | |
B | GLU214 | |
B | TYR230 | |
C | GLU214 | |
C | TYR230 | |
D | GLU214 | |
D | TYR230 | |
E | GLU214 |
site_id | SWS_FT_FI3 |
Number of Residues | 30 |
Details | BINDING: BINDING => ECO:0000305|PubMed:16027359, ECO:0000305|PubMed:19695264, ECO:0000305|PubMed:22369127, ECO:0000305|DOI:10.1039/C2MD00310D, ECO:0007744|PDB:2BVC, ECO:0007744|PDB:2WHI, ECO:0007744|PDB:3ZXR, ECO:0007744|PDB:3ZXV, ECO:0007744|PDB:4ACF |
Chain | Residue | Details |
A | ASN271 | |
B | ARG368 | |
C | ASN271 | |
C | HIS278 | |
C | ARG329 | |
C | ARG347 | |
C | ARG368 | |
D | ASN271 | |
D | HIS278 | |
D | ARG329 | |
D | ARG347 | |
A | HIS278 | |
D | ARG368 | |
E | ASN271 | |
E | HIS278 | |
E | ARG329 | |
E | ARG347 | |
E | ARG368 | |
F | ASN271 | |
F | HIS278 | |
F | ARG329 | |
F | ARG347 | |
A | ARG329 | |
F | ARG368 | |
A | ARG347 | |
A | ARG368 | |
B | ASN271 | |
B | HIS278 | |
B | ARG329 | |
B | ARG347 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P12425 |
Chain | Residue | Details |
A | GLY272 | |
B | GLY272 | |
C | GLY272 | |
D | GLY272 | |
E | GLY272 | |
F | GLY272 |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P77961 |
Chain | Residue | Details |
A | SER280 | |
E | LYS361 | |
F | SER280 | |
F | LYS361 | |
A | LYS361 | |
B | SER280 | |
B | LYS361 | |
C | SER280 | |
C | LYS361 | |
D | SER280 | |
D | LYS361 | |
E | SER280 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0A1P6 |
Chain | Residue | Details |
A | GLU335 | |
B | GLU335 | |
C | GLU335 | |
D | GLU335 | |
E | GLU335 | |
F | GLU335 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:16027359, ECO:0000305|PubMed:22369127, ECO:0000305|DOI:10.1039/C2MD00310D, ECO:0007744|PDB:2BVC, ECO:0007744|PDB:3ZXR, ECO:0007744|PDB:3ZXV, ECO:0007744|PDB:4ACF |
Chain | Residue | Details |
A | ARG352 | |
B | ARG352 | |
C | ARG352 | |
D | ARG352 | |
E | ARG352 | |
F | ARG352 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | MOD_RES: O-AMP-tyrosine => ECO:0000269|PubMed:15037612, ECO:0000305|PubMed:12146952, ECO:0000305|PubMed:16027359 |
Chain | Residue | Details |
A | TYR406 | |
B | TYR406 | |
C | TYR406 | |
D | TYR406 | |
E | TYR406 | |
F | TYR406 |
Catalytic Information from CSA
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 |