2WGS
Crystal structure of Mycobacterium Tuberculosis Glutamine Synthetase in complex with a purine analogue inhibitor.
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 |
| G | 0000287 | molecular_function | magnesium ion binding |
| G | 0001968 | molecular_function | fibronectin binding |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0004356 | molecular_function | glutamine synthetase activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0005576 | cellular_component | extracellular region |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005829 | cellular_component | cytosol |
| G | 0005886 | cellular_component | plasma membrane |
| G | 0006542 | biological_process | glutamine biosynthetic process |
| G | 0009274 | cellular_component | peptidoglycan-based cell wall |
| G | 0010756 | biological_process | positive regulation of plasminogen activation |
| G | 0016020 | cellular_component | membrane |
| G | 0016874 | molecular_function | ligase activity |
| G | 0019740 | biological_process | nitrogen utilization |
| G | 0035375 | molecular_function | zymogen binding |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0051260 | biological_process | protein homooligomerization |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0001968 | molecular_function | fibronectin binding |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0004356 | molecular_function | glutamine synthetase activity |
| H | 0005524 | molecular_function | ATP binding |
| H | 0005576 | cellular_component | extracellular region |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005829 | cellular_component | cytosol |
| H | 0005886 | cellular_component | plasma membrane |
| H | 0006542 | biological_process | glutamine biosynthetic process |
| H | 0009274 | cellular_component | peptidoglycan-based cell wall |
| H | 0010756 | biological_process | positive regulation of plasminogen activation |
| H | 0016020 | cellular_component | membrane |
| H | 0016874 | molecular_function | ligase activity |
| H | 0019740 | biological_process | nitrogen utilization |
| H | 0035375 | molecular_function | zymogen binding |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0051260 | biological_process | protein homooligomerization |
| I | 0000287 | molecular_function | magnesium ion binding |
| I | 0001968 | molecular_function | fibronectin binding |
| I | 0003824 | molecular_function | catalytic activity |
| I | 0004356 | molecular_function | glutamine synthetase activity |
| I | 0005524 | molecular_function | ATP binding |
| I | 0005576 | cellular_component | extracellular region |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0005829 | cellular_component | cytosol |
| I | 0005886 | cellular_component | plasma membrane |
| I | 0006542 | biological_process | glutamine biosynthetic process |
| I | 0009274 | cellular_component | peptidoglycan-based cell wall |
| I | 0010756 | biological_process | positive regulation of plasminogen activation |
| I | 0016020 | cellular_component | membrane |
| I | 0016874 | molecular_function | ligase activity |
| I | 0019740 | biological_process | nitrogen utilization |
| I | 0035375 | molecular_function | zymogen binding |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0051260 | biological_process | protein homooligomerization |
| J | 0000287 | molecular_function | magnesium ion binding |
| J | 0001968 | molecular_function | fibronectin binding |
| J | 0003824 | molecular_function | catalytic activity |
| J | 0004356 | molecular_function | glutamine synthetase activity |
| J | 0005524 | molecular_function | ATP binding |
| J | 0005576 | cellular_component | extracellular region |
| J | 0005737 | cellular_component | cytoplasm |
| J | 0005829 | cellular_component | cytosol |
| J | 0005886 | cellular_component | plasma membrane |
| J | 0006542 | biological_process | glutamine biosynthetic process |
| J | 0009274 | cellular_component | peptidoglycan-based cell wall |
| J | 0010756 | biological_process | positive regulation of plasminogen activation |
| J | 0016020 | cellular_component | membrane |
| J | 0016874 | molecular_function | ligase activity |
| J | 0019740 | biological_process | nitrogen utilization |
| J | 0035375 | molecular_function | zymogen binding |
| J | 0046872 | molecular_function | metal ion binding |
| J | 0051260 | biological_process | protein homooligomerization |
| K | 0000287 | molecular_function | magnesium ion binding |
| K | 0001968 | molecular_function | fibronectin binding |
| K | 0003824 | molecular_function | catalytic activity |
| K | 0004356 | molecular_function | glutamine synthetase activity |
| K | 0005524 | molecular_function | ATP binding |
| K | 0005576 | cellular_component | extracellular region |
| K | 0005737 | cellular_component | cytoplasm |
| K | 0005829 | cellular_component | cytosol |
| K | 0005886 | cellular_component | plasma membrane |
| K | 0006542 | biological_process | glutamine biosynthetic process |
| K | 0009274 | cellular_component | peptidoglycan-based cell wall |
| K | 0010756 | biological_process | positive regulation of plasminogen activation |
| K | 0016020 | cellular_component | membrane |
| K | 0016874 | molecular_function | ligase activity |
| K | 0019740 | biological_process | nitrogen utilization |
| K | 0035375 | molecular_function | zymogen binding |
| K | 0046872 | molecular_function | metal ion binding |
| K | 0051260 | biological_process | protein homooligomerization |
| L | 0000287 | molecular_function | magnesium ion binding |
| L | 0001968 | molecular_function | fibronectin binding |
| L | 0003824 | molecular_function | catalytic activity |
| L | 0004356 | molecular_function | glutamine synthetase activity |
| L | 0005524 | molecular_function | ATP binding |
| L | 0005576 | cellular_component | extracellular region |
| L | 0005737 | cellular_component | cytoplasm |
| L | 0005829 | cellular_component | cytosol |
| L | 0005886 | cellular_component | plasma membrane |
| L | 0006542 | biological_process | glutamine biosynthetic process |
| L | 0009274 | cellular_component | peptidoglycan-based cell wall |
| L | 0010756 | biological_process | positive regulation of plasminogen activation |
| L | 0016020 | cellular_component | membrane |
| L | 0016874 | molecular_function | ligase activity |
| L | 0019740 | biological_process | nitrogen utilization |
| L | 0035375 | molecular_function | zymogen 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 | 11 |
| Details | BINDING SITE FOR RESIDUE 1AZ A 501 |
| Chain | Residue |
| A | TYR129 |
| A | LYS361 |
| A | ARG364 |
| A | GLY131 |
| A | GLU133 |
| A | ASN229 |
| A | TYR230 |
| A | PHE232 |
| A | HIS278 |
| A | SER280 |
| A | TRP282 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 502 |
| Chain | Residue |
| A | LEU423 |
| A | SER424 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1AZ B 501 |
| Chain | Residue |
| B | TYR129 |
| B | PHE130 |
| B | GLY131 |
| B | GLU133 |
| B | ASN229 |
| B | TYR230 |
| B | PHE232 |
| B | HIS278 |
| B | SER280 |
| B | TRP282 |
| B | LYS361 |
| B | ARG364 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 502 |
| Chain | Residue |
| B | LEU423 |
| B | SER424 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1AZ C 501 |
| Chain | Residue |
| C | TYR129 |
| C | PHE130 |
| C | GLY131 |
| C | GLU133 |
| C | ASN229 |
| C | TYR230 |
| C | PHE232 |
| C | HIS278 |
| C | SER280 |
| C | TRP282 |
| C | LYS361 |
| C | ARG364 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 502 |
| Chain | Residue |
| C | LEU423 |
| C | SER424 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1AZ D 501 |
| Chain | Residue |
| D | TYR129 |
| D | PHE130 |
| D | GLY131 |
| D | GLU133 |
| D | ASN229 |
| D | TYR230 |
| D | PHE232 |
| D | HIS278 |
| D | SER280 |
| D | TRP282 |
| D | LYS361 |
| D | ARG364 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 502 |
| Chain | Residue |
| D | LEU423 |
| D | SER424 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1AZ E 501 |
| Chain | Residue |
| E | TYR129 |
| E | PHE130 |
| E | GLY131 |
| E | GLU133 |
| E | ASN229 |
| E | TYR230 |
| E | PHE232 |
| E | HIS278 |
| E | SER280 |
| E | TRP282 |
| E | LYS361 |
| E | ARG364 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL E 502 |
| Chain | Residue |
| E | LEU423 |
| E | SER424 |
| E | HOH2120 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1AZ F 501 |
| Chain | Residue |
| F | TYR129 |
| F | PHE130 |
| F | GLY131 |
| F | GLU133 |
| F | ASN229 |
| F | TYR230 |
| F | PHE232 |
| F | HIS278 |
| F | SER280 |
| F | TRP282 |
| F | LYS361 |
| F | ARG364 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL F 502 |
| Chain | Residue |
| F | LEU423 |
| F | SER424 |
| site_id | BC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 1AZ G 501 |
| Chain | Residue |
| G | TYR129 |
| G | GLY131 |
| G | GLU133 |
| G | ASN229 |
| G | TYR230 |
| G | PHE232 |
| G | HIS278 |
| G | SER280 |
| G | TRP282 |
| G | LYS361 |
| G | ARG364 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL G 502 |
| Chain | Residue |
| G | LEU423 |
| G | SER424 |
| site_id | BC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 1AZ H 501 |
| Chain | Residue |
| H | GLU133 |
| H | ASN229 |
| H | TYR230 |
| H | PHE232 |
| H | HIS278 |
| H | SER280 |
| H | TRP282 |
| H | LYS361 |
| H | ARG364 |
| H | TYR129 |
| H | GLY131 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL H 502 |
| Chain | Residue |
| H | LEU423 |
| H | SER424 |
| site_id | BC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1AZ I 501 |
| Chain | Residue |
| I | TYR129 |
| I | PHE130 |
| I | GLY131 |
| I | GLU133 |
| I | ASN229 |
| I | TYR230 |
| I | PHE232 |
| I | HIS278 |
| I | SER280 |
| I | TRP282 |
| I | LYS361 |
| I | ARG364 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL I 502 |
| Chain | Residue |
| I | LEU423 |
| I | SER424 |
| site_id | CC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1AZ J 501 |
| Chain | Residue |
| J | TYR129 |
| J | PHE130 |
| J | GLY131 |
| J | GLU133 |
| J | ASN229 |
| J | TYR230 |
| J | PHE232 |
| J | HIS278 |
| J | SER280 |
| J | TRP282 |
| J | LYS361 |
| J | ARG364 |
| site_id | CC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL J 502 |
| Chain | Residue |
| J | LEU423 |
| J | SER424 |
| site_id | CC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1AZ K 501 |
| Chain | Residue |
| K | TYR129 |
| K | PHE130 |
| K | GLY131 |
| K | GLU133 |
| K | ASN229 |
| K | TYR230 |
| K | PHE232 |
| K | HIS278 |
| K | SER280 |
| K | TRP282 |
| K | LYS361 |
| K | ARG364 |
| site_id | CC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL K 502 |
| Chain | Residue |
| K | LEU423 |
| K | SER424 |
| site_id | CC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1AZ L 501 |
| Chain | Residue |
| L | TYR129 |
| L | PHE130 |
| L | GLY131 |
| L | GLU133 |
| L | ASN229 |
| L | TYR230 |
| L | PHE232 |
| L | HIS278 |
| L | SER280 |
| L | TRP282 |
| L | LYS361 |
| L | ARG364 |
| site_id | CC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL L 502 |
| Chain | Residue |
| L | LEU423 |
| L | SER424 |
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 | 72 |
| 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 | |
| G | GLU133 | |
| G | GLU135 | |
| G | GLU219 | |
| A | GLU227 | |
| G | GLU227 | |
| G | HIS276 | |
| G | GLU366 | |
| H | GLU133 | |
| H | GLU135 | |
| H | GLU219 | |
| H | GLU227 | |
| H | HIS276 | |
| H | GLU366 | |
| I | GLU133 | |
| A | HIS276 | |
| I | GLU135 | |
| I | GLU219 | |
| I | GLU227 | |
| I | HIS276 | |
| I | GLU366 | |
| J | GLU133 | |
| J | GLU135 | |
| J | GLU219 | |
| J | GLU227 | |
| J | HIS276 | |
| A | GLU366 | |
| J | GLU366 | |
| K | GLU133 | |
| K | GLU135 | |
| K | GLU219 | |
| K | GLU227 | |
| K | HIS276 | |
| K | GLU366 | |
| L | GLU133 | |
| L | GLU135 | |
| L | GLU219 | |
| B | GLU133 | |
| L | GLU227 | |
| L | HIS276 | |
| L | GLU366 | |
| B | GLU135 | |
| B | GLU219 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:16027359, ECO:0007744|PDB:2BVC |
| Chain | Residue | Details |
| A | GLU214 | |
| E | TYR230 | |
| F | GLU214 | |
| F | TYR230 | |
| G | GLU214 | |
| G | TYR230 | |
| H | GLU214 | |
| H | TYR230 | |
| I | GLU214 | |
| I | TYR230 | |
| J | GLU214 | |
| A | TYR230 | |
| J | TYR230 | |
| K | GLU214 | |
| K | TYR230 | |
| L | GLU214 | |
| L | TYR230 | |
| B | GLU214 | |
| B | TYR230 | |
| C | GLU214 | |
| C | TYR230 | |
| D | GLU214 | |
| D | TYR230 | |
| E | GLU214 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 60 |
| 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 | |
| G | ASN271 | |
| G | HIS278 | |
| G | ARG329 | |
| G | ARG347 | |
| G | ARG368 | |
| H | ASN271 | |
| H | HIS278 | |
| H | ARG329 | |
| H | ARG347 | |
| A | ARG347 | |
| H | ARG368 | |
| I | ASN271 | |
| I | HIS278 | |
| I | ARG329 | |
| I | ARG347 | |
| I | ARG368 | |
| J | ASN271 | |
| J | HIS278 | |
| J | ARG329 | |
| J | ARG347 | |
| A | ARG368 | |
| J | ARG368 | |
| K | ASN271 | |
| K | HIS278 | |
| K | ARG329 | |
| K | ARG347 | |
| K | ARG368 | |
| L | ASN271 | |
| L | HIS278 | |
| L | ARG329 | |
| L | ARG347 | |
| B | ASN271 | |
| L | ARG368 | |
| B | HIS278 | |
| B | ARG329 | |
| B | ARG347 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P12425 |
| Chain | Residue | Details |
| A | GLY272 | |
| J | GLY272 | |
| K | GLY272 | |
| L | GLY272 | |
| B | GLY272 | |
| C | GLY272 | |
| D | GLY272 | |
| E | GLY272 | |
| F | GLY272 | |
| G | GLY272 | |
| H | GLY272 | |
| I | GLY272 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P77961 |
| Chain | Residue | Details |
| A | SER280 | |
| E | LYS361 | |
| F | SER280 | |
| F | LYS361 | |
| G | SER280 | |
| G | LYS361 | |
| H | SER280 | |
| H | LYS361 | |
| I | SER280 | |
| I | LYS361 | |
| J | SER280 | |
| A | LYS361 | |
| J | LYS361 | |
| K | SER280 | |
| K | LYS361 | |
| L | SER280 | |
| L | LYS361 | |
| B | SER280 | |
| B | LYS361 | |
| C | SER280 | |
| C | LYS361 | |
| D | SER280 | |
| D | LYS361 | |
| E | SER280 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0A1P6 |
| Chain | Residue | Details |
| A | GLU335 | |
| J | GLU335 | |
| K | GLU335 | |
| L | GLU335 | |
| B | GLU335 | |
| C | GLU335 | |
| D | GLU335 | |
| E | GLU335 | |
| F | GLU335 | |
| G | GLU335 | |
| H | GLU335 | |
| I | GLU335 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| 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 | |
| J | ARG352 | |
| K | ARG352 | |
| L | ARG352 | |
| B | ARG352 | |
| C | ARG352 | |
| D | ARG352 | |
| E | ARG352 | |
| F | ARG352 | |
| G | ARG352 | |
| H | ARG352 | |
| I | ARG352 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 12 |
| Details | MOD_RES: O-AMP-tyrosine => ECO:0000269|PubMed:15037612, ECO:0000305|PubMed:12146952, ECO:0000305|PubMed:16027359 |
| Chain | Residue | Details |
| A | TYR406 | |
| J | TYR406 | |
| K | TYR406 | |
| L | TYR406 | |
| B | TYR406 | |
| C | TYR406 | |
| D | TYR406 | |
| E | TYR406 | |
| F | TYR406 | |
| G | TYR406 | |
| H | TYR406 | |
| I | TYR406 |
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 | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| J | ASP54 | |
| J | ARG347 | |
| J | GLU335 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| K | ASP54 | |
| K | ARG347 | |
| K | GLU335 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| L | ASP54 | |
| L | ARG347 | |
| L | 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 | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| G | ASP54 | |
| G | ARG347 | |
| G | GLU335 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| H | ASP54 | |
| H | ARG347 | |
| H | GLU335 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hto |
| Chain | Residue | Details |
| I | ASP54 | |
| I | ARG347 | |
| I | 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 | MCSA10 |
| Number of Residues | 9 |
| Details | M-CSA 537 |
| Chain | Residue | Details |
| J | ASP54 | activator, proton acceptor |
| J | GLU133 | metal ligand |
| J | GLU135 | metal ligand |
| J | GLU219 | metal ligand |
| J | GLU227 | metal ligand |
| J | HIS276 | metal ligand |
| J | ARG347 | electrostatic stabiliser |
| J | GLU366 | metal ligand |
| J | ARG368 | electrostatic stabiliser |
| site_id | MCSA11 |
| Number of Residues | 9 |
| Details | M-CSA 537 |
| Chain | Residue | Details |
| K | ASP54 | activator, proton acceptor |
| K | GLU133 | metal ligand |
| K | GLU135 | metal ligand |
| K | GLU219 | metal ligand |
| K | GLU227 | metal ligand |
| K | HIS276 | metal ligand |
| K | ARG347 | electrostatic stabiliser |
| K | GLU366 | metal ligand |
| K | ARG368 | electrostatic stabiliser |
| site_id | MCSA12 |
| Number of Residues | 9 |
| Details | M-CSA 537 |
| Chain | Residue | Details |
| L | ASP54 | activator, proton acceptor |
| L | GLU133 | metal ligand |
| L | GLU135 | metal ligand |
| L | GLU219 | metal ligand |
| L | GLU227 | metal ligand |
| L | HIS276 | metal ligand |
| L | ARG347 | electrostatic stabiliser |
| L | GLU366 | metal ligand |
| L | 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 |
| site_id | MCSA7 |
| Number of Residues | 9 |
| Details | M-CSA 537 |
| Chain | Residue | Details |
| G | ASP54 | activator, proton acceptor |
| G | GLU133 | metal ligand |
| G | GLU135 | metal ligand |
| G | GLU219 | metal ligand |
| G | GLU227 | metal ligand |
| G | HIS276 | metal ligand |
| G | ARG347 | electrostatic stabiliser |
| G | GLU366 | metal ligand |
| G | ARG368 | electrostatic stabiliser |
| site_id | MCSA8 |
| Number of Residues | 9 |
| Details | M-CSA 537 |
| Chain | Residue | Details |
| H | ASP54 | activator, proton acceptor |
| H | GLU133 | metal ligand |
| H | GLU135 | metal ligand |
| H | GLU219 | metal ligand |
| H | GLU227 | metal ligand |
| H | HIS276 | metal ligand |
| H | ARG347 | electrostatic stabiliser |
| H | GLU366 | metal ligand |
| H | ARG368 | electrostatic stabiliser |
| site_id | MCSA9 |
| Number of Residues | 9 |
| Details | M-CSA 537 |
| Chain | Residue | Details |
| I | ASP54 | activator, proton acceptor |
| I | GLU133 | metal ligand |
| I | GLU135 | metal ligand |
| I | GLU219 | metal ligand |
| I | GLU227 | metal ligand |
| I | HIS276 | metal ligand |
| I | ARG347 | electrostatic stabiliser |
| I | GLU366 | metal ligand |
| I | ARG368 | electrostatic stabiliser |
