2BVC
Crystal structure of Mycobacterium tuberculosis glutamine synthetase in complex with a transition state mimic
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 | 5 |
Details | BINDING SITE FOR RESIDUE MG A 502 |
Chain | Residue |
A | GLU135 |
A | GLU219 |
A | GLU227 |
A | P3S500 |
A | HOH2028 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 503 |
Chain | Residue |
A | ADP501 |
A | GLU133 |
A | HIS276 |
A | GLU366 |
A | P3S500 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 504 |
Chain | Residue |
A | GLU133 |
A | GLU227 |
A | P3S500 |
A | ADP501 |
A | HOH2067 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 505 |
Chain | Residue |
F | SER424 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 502 |
Chain | Residue |
B | GLU135 |
B | GLU219 |
B | GLU227 |
B | P3S500 |
B | HOH2091 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 503 |
Chain | Residue |
B | GLU133 |
B | HIS276 |
B | GLU366 |
B | ARG368 |
B | P3S500 |
B | ADP501 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 504 |
Chain | Residue |
B | GLU133 |
B | GLU227 |
B | P3S500 |
B | ADP501 |
B | HOH2057 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 505 |
Chain | Residue |
E | SER424 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 502 |
Chain | Residue |
C | GLU135 |
C | GLU219 |
C | GLU227 |
C | P3S500 |
C | HOH2087 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 503 |
Chain | Residue |
C | GLU133 |
C | HIS276 |
C | GLU366 |
C | ARG368 |
C | P3S500 |
C | ADP501 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 504 |
Chain | Residue |
C | GLU133 |
C | GLU227 |
C | P3S500 |
C | ADP501 |
C | HOH2053 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL C 505 |
Chain | Residue |
A | SER424 |
A | HOH2109 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 502 |
Chain | Residue |
D | GLU135 |
D | GLU219 |
D | GLU227 |
D | P3S500 |
D | HOH2063 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 503 |
Chain | Residue |
D | GLU133 |
D | HIS276 |
D | GLU366 |
D | ARG368 |
D | P3S500 |
D | ADP501 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 504 |
Chain | Residue |
D | GLU133 |
D | GLU227 |
D | P3S500 |
D | ADP501 |
D | HOH2059 |
site_id | BC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL D 505 |
Chain | Residue |
B | SER424 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG E 502 |
Chain | Residue |
E | GLU135 |
E | GLU219 |
E | GLU227 |
E | P3S500 |
E | MG504 |
E | HOH2073 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG E 503 |
Chain | Residue |
E | GLU133 |
E | HIS276 |
E | GLU366 |
E | P3S500 |
E | ADP501 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG E 504 |
Chain | Residue |
E | GLU133 |
E | GLU227 |
E | P3S500 |
E | ADP501 |
E | MG502 |
E | HOH2074 |
site_id | CC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL E 505 |
Chain | Residue |
C | SER424 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG F 502 |
Chain | Residue |
F | GLU135 |
F | GLU219 |
F | GLU227 |
F | P3S500 |
F | MG504 |
F | HOH2027 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG F 503 |
Chain | Residue |
F | GLU133 |
F | HIS276 |
F | GLU366 |
F | P3S500 |
F | ADP501 |
site_id | CC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG F 504 |
Chain | Residue |
F | P3S500 |
F | ADP501 |
F | MG502 |
F | HOH2105 |
F | GLU133 |
F | GLU227 |
site_id | CC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL F 505 |
Chain | Residue |
D | SER424 |
site_id | CC7 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE P3S A 500 |
Chain | Residue |
A | GLU133 |
A | GLU135 |
A | GLU219 |
A | GLU227 |
A | GLY272 |
A | HIS276 |
A | ARG329 |
A | TYR334 |
A | GLU335 |
A | ARG347 |
A | GLU366 |
A | ARG368 |
A | ADP501 |
A | MG502 |
A | MG503 |
A | MG504 |
A | HOH2028 |
A | HOH2047 |
A | HOH2067 |
A | HOH2116 |
A | HOH2117 |
F | ASP54 |
site_id | CC8 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE ADP A 501 |
Chain | Residue |
A | GLU133 |
A | GLU214 |
A | LYS215 |
A | GLU227 |
A | ASN229 |
A | TYR230 |
A | GLN231 |
A | PHE232 |
A | HIS278 |
A | SER280 |
A | ARG347 |
A | ARG352 |
A | LYS361 |
A | ARG364 |
A | GLU366 |
A | P3S500 |
A | MG503 |
A | MG504 |
A | HOH2025 |
A | HOH2067 |
A | HOH2094 |
A | HOH2118 |
A | HOH2119 |
site_id | CC9 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE P3S B 500 |
Chain | Residue |
A | ASP54 |
B | GLU133 |
B | GLU135 |
B | GLU219 |
B | GLU227 |
B | GLY272 |
B | HIS276 |
B | ARG329 |
B | GLU335 |
B | ARG347 |
B | GLU366 |
B | ARG368 |
B | ADP501 |
B | MG502 |
B | MG503 |
B | MG504 |
B | HOH2038 |
B | HOH2076 |
B | HOH2091 |
B | HOH2092 |
site_id | DC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ADP B 501 |
Chain | Residue |
B | GLU133 |
B | GLU214 |
B | LYS215 |
B | GLU227 |
B | ASN229 |
B | TYR230 |
B | GLN231 |
B | PHE232 |
B | HIS278 |
B | SER280 |
B | ARG347 |
B | ARG352 |
B | LYS361 |
B | ARG364 |
B | GLU366 |
B | P3S500 |
B | MG503 |
B | MG504 |
B | HOH2014 |
B | HOH2055 |
B | HOH2057 |
site_id | DC2 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE P3S C 500 |
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 | ADP501 |
C | MG502 |
C | MG503 |
C | MG504 |
C | HOH2038 |
C | HOH2053 |
C | HOH2069 |
C | HOH2086 |
C | HOH2087 |
site_id | DC3 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE ADP C 501 |
Chain | Residue |
C | GLU133 |
C | GLU214 |
C | LYS215 |
C | GLU227 |
C | ASN229 |
C | TYR230 |
C | GLN231 |
C | PHE232 |
C | HIS278 |
C | SER280 |
C | ARG347 |
C | ARG352 |
C | LYS361 |
C | ARG364 |
C | GLU366 |
C | P3S500 |
C | MG503 |
C | MG504 |
C | HOH2015 |
C | HOH2053 |
site_id | DC4 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE P3S D 500 |
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 | ADP501 |
D | MG502 |
D | MG503 |
D | MG504 |
D | HOH2059 |
D | HOH2061 |
D | HOH2063 |
D | HOH2078 |
D | HOH2096 |
site_id | DC5 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ADP D 501 |
Chain | Residue |
D | GLU133 |
D | GLU214 |
D | LYS215 |
D | GLU227 |
D | ASN229 |
D | TYR230 |
D | GLN231 |
D | PHE232 |
D | HIS278 |
D | SER280 |
D | ARG347 |
D | ARG352 |
D | LYS361 |
D | ARG364 |
D | GLU366 |
D | P3S500 |
D | MG503 |
D | MG504 |
D | HOH2024 |
D | HOH2058 |
D | HOH2059 |
site_id | DC6 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE P3S E 500 |
Chain | Residue |
D | ASP54 |
E | GLU133 |
E | GLU135 |
E | GLU219 |
E | GLU227 |
E | GLY272 |
E | GLY274 |
E | HIS276 |
E | ARG329 |
E | GLU335 |
E | ARG347 |
E | GLU366 |
E | ARG368 |
E | ADP501 |
E | MG502 |
E | MG503 |
E | MG504 |
E | HOH2051 |
E | HOH2072 |
E | HOH2073 |
E | HOH2074 |
E | HOH2094 |
site_id | DC7 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ADP E 501 |
Chain | Residue |
E | GLY131 |
E | GLU133 |
E | GLU214 |
E | LYS215 |
E | GLU227 |
E | ASN229 |
E | TYR230 |
E | GLN231 |
E | PHE232 |
E | HIS278 |
E | SER280 |
E | ARG347 |
E | ARG352 |
E | LYS361 |
E | ARG364 |
E | GLU366 |
E | P3S500 |
E | MG503 |
E | MG504 |
E | HOH2074 |
E | HOH2101 |
E | HOH2121 |
site_id | DC8 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE P3S F 500 |
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 | ADP501 |
F | MG502 |
F | MG503 |
F | MG504 |
F | HOH2027 |
F | HOH2065 |
F | HOH2081 |
F | HOH2105 |
F | HOH2106 |
site_id | DC9 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE ADP F 501 |
Chain | Residue |
F | GLU133 |
F | GLU214 |
F | LYS215 |
F | GLU227 |
F | ASN229 |
F | TYR230 |
F | GLN231 |
F | PHE232 |
F | HIS278 |
F | SER280 |
F | ARG347 |
F | ARG352 |
F | LYS361 |
F | ARG364 |
F | GLU366 |
F | P3S500 |
F | MG503 |
F | MG504 |
F | HOH2025 |
F | HOH2105 |
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 | 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 |