Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001968molecular_functionfibronectin binding
A0003824molecular_functioncatalytic activity
A0004356molecular_functionglutamine synthetase activity
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006542biological_processglutamine biosynthetic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0010756biological_processpositive regulation of plasminogen activation
A0016020cellular_componentmembrane
A0016874molecular_functionligase activity
A0019740biological_processnitrogen utilization
A0035375molecular_functionzymogen binding
A0046872molecular_functionmetal ion binding
A0051260biological_processprotein homooligomerization
B0000287molecular_functionmagnesium ion binding
B0001968molecular_functionfibronectin binding
B0003824molecular_functioncatalytic activity
B0004356molecular_functionglutamine synthetase activity
B0005524molecular_functionATP binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006542biological_processglutamine biosynthetic process
B0009274cellular_componentpeptidoglycan-based cell wall
B0010756biological_processpositive regulation of plasminogen activation
B0016020cellular_componentmembrane
B0016874molecular_functionligase activity
B0019740biological_processnitrogen utilization
B0035375molecular_functionzymogen binding
B0046872molecular_functionmetal ion binding
B0051260biological_processprotein homooligomerization
C0000287molecular_functionmagnesium ion binding
C0001968molecular_functionfibronectin binding
C0003824molecular_functioncatalytic activity
C0004356molecular_functionglutamine synthetase activity
C0005524molecular_functionATP binding
C0005576cellular_componentextracellular region
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006542biological_processglutamine biosynthetic process
C0009274cellular_componentpeptidoglycan-based cell wall
C0010756biological_processpositive regulation of plasminogen activation
C0016020cellular_componentmembrane
C0016874molecular_functionligase activity
C0019740biological_processnitrogen utilization
C0035375molecular_functionzymogen binding
C0046872molecular_functionmetal ion binding
C0051260biological_processprotein homooligomerization
D0000287molecular_functionmagnesium ion binding
D0001968molecular_functionfibronectin binding
D0003824molecular_functioncatalytic activity
D0004356molecular_functionglutamine synthetase activity
D0005524molecular_functionATP binding
D0005576cellular_componentextracellular region
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006542biological_processglutamine biosynthetic process
D0009274cellular_componentpeptidoglycan-based cell wall
D0010756biological_processpositive regulation of plasminogen activation
D0016020cellular_componentmembrane
D0016874molecular_functionligase activity
D0019740biological_processnitrogen utilization
D0035375molecular_functionzymogen binding
D0046872molecular_functionmetal ion binding
D0051260biological_processprotein homooligomerization
E0000287molecular_functionmagnesium ion binding
E0001968molecular_functionfibronectin binding
E0003824molecular_functioncatalytic activity
E0004356molecular_functionglutamine synthetase activity
E0005524molecular_functionATP binding
E0005576cellular_componentextracellular region
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0005886cellular_componentplasma membrane
E0006542biological_processglutamine biosynthetic process
E0009274cellular_componentpeptidoglycan-based cell wall
E0010756biological_processpositive regulation of plasminogen activation
E0016020cellular_componentmembrane
E0016874molecular_functionligase activity
E0019740biological_processnitrogen utilization
E0035375molecular_functionzymogen binding
E0046872molecular_functionmetal ion binding
E0051260biological_processprotein homooligomerization
F0000287molecular_functionmagnesium ion binding
F0001968molecular_functionfibronectin binding
F0003824molecular_functioncatalytic activity
F0004356molecular_functionglutamine synthetase activity
F0005524molecular_functionATP binding
F0005576cellular_componentextracellular region
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0005886cellular_componentplasma membrane
F0006542biological_processglutamine biosynthetic process
F0009274cellular_componentpeptidoglycan-based cell wall
F0010756biological_processpositive regulation of plasminogen activation
F0016020cellular_componentmembrane
F0016874molecular_functionligase activity
F0019740biological_processnitrogen utilization
F0035375molecular_functionzymogen binding
F0046872molecular_functionmetal ion binding
F0051260biological_processprotein homooligomerization
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 46B A 1479
ChainResidue
ATYR129
APHE232
AHIS278
ATRP282
AASN359
ALYS361
AARG364
AHOH2248

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1480
ChainResidue
AGLU219
AGLU227
AP3S1483
AHOH2123
AGLU135

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1481
ChainResidue
AGLU133
AHIS276
AGLU366
AARG368
AP3S1483
APO41484

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 1482
ChainResidue
AGLU133
AGLU227
AASN229
AP3S1483
APO41484
AHOH2124
AHOH2217

site_idAC5
Number of Residues22
DetailsBINDING SITE FOR RESIDUE P3S A 1483
ChainResidue
AGLU133
AGLU135
AGLU219
AGLU227
AGLY272
AGLY274
AHIS276
AARG329
AGLU335
AARG347
AGLU366
AARG368
AMG1480
AMG1481
AMG1482
APO41484
AHOH2123
AHOH2182
AHOH2217
AHOH2220
AHOH2246
FASP54

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 A 1484
ChainResidue
AGLU133
AHIS278
AARG347
AARG352
AGLU366
AMG1481
AMG1482
AP3S1483
AHOH2124
AHOH2217
AHOH2218
AHOH2300

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1485
ChainResidue
ASER424

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1486
ChainResidue
AHIS237
AHOH2067
AHOH2068
AHOH2224
AHOH2225
AHOH2349

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 46B B 1479
ChainResidue
BTYR129
BGLY131
BPHE232
BHIS278
BTRP282
BASN359
BLYS361
BARG364
BHOH2229
ELYS14

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1480
ChainResidue
BGLU135
BGLU219
BGLU227
BP3S1483
BHOH2122

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1481
ChainResidue
BGLU133
BHIS276
BGLU366
BP3S1483
BPO41484

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1482
ChainResidue
BGLU133
BGLU227
BP3S1483
BPO41484
BHOH2121
BHOH2200

site_idBC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE P3S B 1483
ChainResidue
BHIS276
BARG329
BGLU335
BARG347
BGLU366
BARG368
BMG1480
BMG1481
BMG1482
BPO41484
BHOH2122
BHOH2174
BHOH2200
BHOH2201
BHOH2227
AASP54
BGLU133
BGLU135
BGLU219
BGLU227
BGLY272

site_idBC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 B 1484
ChainResidue
BGLU133
BHIS278
BARG347
BARG352
BGLU366
BMG1481
BMG1482
BP3S1483
BHOH2121
BHOH2199
BHOH2200
BHOH2277

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 1485
ChainResidue
BSER424
BHOH2320

site_idBC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 1486
ChainResidue
BGLU76
BHIS237
BHOH2065
BHOH2066
BHOH2205
BHOH2206
BHOH2325

site_idBC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 46B C 1479
ChainResidue
CTYR129
CPHE232
CHIS278
CTRP282
CASN359
CLYS361
CARG364

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 1480
ChainResidue
CGLU135
CGLU219
CGLU227
CP3S1483
CHOH2119

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 1481
ChainResidue
CGLU133
CHIS276
CGLU366
CARG368
CP3S1483
CPO41484

site_idCC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 1482
ChainResidue
CGLU133
CGLU227
CP3S1483
CPO41484
CHOH2118
CHOH2195

site_idCC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE P3S C 1483
ChainResidue
BASP54
CGLU133
CGLU135
CGLU219
CGLU227
CGLY272
CHIS276
CARG329
CTYR334
CGLU335
CARG347
CGLU366
CARG368
CMG1480
CMG1481
CMG1482
CPO41484
CHOH2119
CHOH2171
CHOH2195
CHOH2196
CHOH2223

site_idCC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 C 1484
ChainResidue
CGLU133
CHIS278
CARG347
CARG352
CGLU366
CMG1481
CMG1482
CP3S1483
CHOH2118
CHOH2194
CHOH2195
CHOH2273

site_idCC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL C 1485
ChainResidue
CLEU423
CSER424

site_idCC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG C 1486
ChainResidue
CGLU76
CHIS237
CHOH2064
CHOH2065
CHOH2200
CHOH2201
CHOH2320

site_idCC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 46B D 1479
ChainResidue
DTYR129
DPHE232
DHIS278
DTRP282
DASN359
DLYS361
DARG364
DHOH2223

site_idCC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 1480
ChainResidue
DGLU135
DGLU219
DGLU227
DMG1482
DP3S1483
DHOH2114

site_idCC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 1481
ChainResidue
DGLU133
DHIS276
DGLU366
DARG368
DP3S1483
DPO41484

site_idDC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG D 1482
ChainResidue
DGLU133
DGLU227
DMG1480
DP3S1483
DPO41484
DHOH2115
DHOH2193

site_idDC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE P3S D 1483
ChainResidue
CASP54
DGLU133
DGLU135
DGLU219
DGLU227
DGLY272
DHIS276
DARG329
DGLU335
DARG347
DGLU366
DARG368
DMG1480
DMG1481
DMG1482
DPO41484
DHOH2114
DHOH2167
DHOH2193
DHOH2194
DHOH2222

site_idDC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PO4 D 1484
ChainResidue
DGLU133
DHIS278
DARG347
DARG352
DGLU366
DMG1481
DMG1482
DP3S1483
DHOH2115
DHOH2193
DHOH2270

site_idDC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL D 1485
ChainResidue
DSER424

site_idDC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG D 1486
ChainResidue
DGLU76
DHIS237
DHOH2061
DHOH2062
DHOH2198
DHOH2199
DHOH2318

site_idDC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 46B E 1479
ChainResidue
ETYR129
EPHE232
EHIS278
ETRP282
EASN359
ELYS361
EARG364
EHOH2224

site_idDC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG E 1480
ChainResidue
EGLU135
EGLU219
EGLU227
EMG1482
EP3S1483
EHOH2116

site_idDC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG E 1481
ChainResidue
EGLU133
EHIS276
EGLU366
EARG368
EP3S1483
EPO41484

site_idDC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG E 1482
ChainResidue
EGLU133
EGLU227
EMG1480
EP3S1483
EPO41484
EHOH2115
EHOH2194

site_idEC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE P3S E 1483
ChainResidue
DASP54
EGLU133
EGLU135
EGLU219
EGLU227
EGLY272
EHIS276
EARG329
ETYR334
EGLU335
EARG347
EGLU366
EARG368
EMG1480
EMG1481
EMG1482
EPO41484
EHOH2116
EHOH2169
EHOH2194
EHOH2196
EHOH2222

site_idEC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 E 1484
ChainResidue
EGLU133
EHIS278
EARG347
EARG352
EGLU366
EMG1481
EMG1482
EP3S1483
EHOH2115
EHOH2194
EHOH2195
EHOH2272

site_idEC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL E 1485
ChainResidue
ESER424

site_idEC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG E 1486
ChainResidue
EGLU76
EHIS237
EHOH2064
EHOH2065
EHOH2200
EHOH2201
EHOH2320

site_idEC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 46B F 1479
ChainResidue
FTYR129
FPHE232
FHIS278
FTRP282
FASN359
FLYS361
FARG364
FHOH2199

site_idEC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG F 1480
ChainResidue
FGLU135
FGLU219
FGLU227
FMG1482
FP3S1483
FHOH2095

site_idEC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG F 1481
ChainResidue
FGLU133
FHIS276
FGLU366
FP3S1483
FPO41484

site_idEC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG F 1482
ChainResidue
FGLU133
FGLU227
FMG1480
FP3S1483
FPO41484
FHOH2096
FHOH2171

site_idEC9
Number of Residues23
DetailsBINDING SITE FOR RESIDUE P3S F 1483
ChainResidue
EASP54
FGLU133
FGLU135
FGLU219
FGLU227
FGLY272
FGLY274
FHIS276
FARG329
FGLU335
FALA336
FARG347
FGLU366
FARG368
FMG1480
FMG1481
FMG1482
FPO41484
FHOH2095
FHOH2147
FHOH2171
FHOH2173
FHOH2197

site_idFC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 F 1484
ChainResidue
FGLU133
FHIS278
FARG347
FARG352
FGLU366
FMG1481
FMG1482
FP3S1483
FHOH2096
FHOH2171
FHOH2172
FHOH2247

site_idFC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL F 1485
ChainResidue
FSER424

site_idFC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG F 1486
ChainResidue
FHIS237
FHOH2046
FHOH2047
FHOH2177
FHOH2178
FHOH2294

Functional Information from PROSITE/UniProt
site_idPS00180
Number of Residues19
DetailsGLNA_1 Glutamine synthetase signature 1. FDGSSirgfqsihESDmlL
ChainResidueDetails
APHE53-LEU71

site_idPS00181
Number of Residues16
DetailsGLNA_ATP Glutamine synthetase putative ATP-binding region signature. KPLfgd..NGSGmHchqS
ChainResidueDetails
ALYS265-SER280

site_idPS00182
Number of Residues13
DetailsGLNA_ADENYLATION Glutamine synthetase class-I adenylation site. KIepqapVDKDLY
ChainResidueDetails
ALYS394-TYR406

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBINDING: 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
ChainResidueDetails
AGLU133
BGLU227
BHIS276
BGLU366
CGLU133
CGLU135
CGLU219
CGLU227
CHIS276
CGLU366
DGLU133
AGLU135
DGLU135
DGLU219
DGLU227
DHIS276
DGLU366
EGLU133
EGLU135
EGLU219
EGLU227
EHIS276
AGLU219
EGLU366
FGLU133
FGLU135
FGLU219
FGLU227
FHIS276
FGLU366
AGLU227
AHIS276
AGLU366
BGLU133
BGLU135
BGLU219

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305|PubMed:16027359, ECO:0007744|PDB:2BVC
ChainResidueDetails
AGLU214
ETYR230
FGLU214
FTYR230
ATYR230
BGLU214
BTYR230
CGLU214
CTYR230
DGLU214
DTYR230
EGLU214

site_idSWS_FT_FI3
Number of Residues30
DetailsBINDING: 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
ChainResidueDetails
AASN271
BARG368
CASN271
CHIS278
CARG329
CARG347
CARG368
DASN271
DHIS278
DARG329
DARG347
AHIS278
DARG368
EASN271
EHIS278
EARG329
EARG347
EARG368
FASN271
FHIS278
FARG329
FARG347
AARG329
FARG368
AARG347
AARG368
BASN271
BHIS278
BARG329
BARG347

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P12425
ChainResidueDetails
AGLY272
BGLY272
CGLY272
DGLY272
EGLY272
FGLY272

site_idSWS_FT_FI5
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P77961
ChainResidueDetails
ASER280
ELYS361
FSER280
FLYS361
ALYS361
BSER280
BLYS361
CSER280
CLYS361
DSER280
DLYS361
ESER280

site_idSWS_FT_FI6
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A1P6
ChainResidueDetails
AGLU335
BGLU335
CGLU335
DGLU335
EGLU335
FGLU335

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: 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
ChainResidueDetails
AARG352
BARG352
CARG352
DARG352
EARG352
FARG352

site_idSWS_FT_FI8
Number of Residues6
DetailsMOD_RES: O-AMP-tyrosine => ECO:0000269|PubMed:15037612, ECO:0000305|PubMed:12146952, ECO:0000305|PubMed:16027359
ChainResidueDetails
ATYR406
BTYR406
CTYR406
DTYR406
ETYR406
FTYR406

Catalytic Information from CSA
site_idMCSA1
Number of Residues9
DetailsM-CSA 537
ChainResidueDetails
AASP54activator, proton acceptor
AGLU133metal ligand
AGLU135metal ligand
AGLU219metal ligand
AGLU227metal ligand
AHIS276metal ligand
AARG347electrostatic stabiliser
AGLU366metal ligand
AARG368electrostatic stabiliser

site_idMCSA2
Number of Residues9
DetailsM-CSA 537
ChainResidueDetails
BASP54activator, proton acceptor
BGLU133metal ligand
BGLU135metal ligand
BGLU219metal ligand
BGLU227metal ligand
BHIS276metal ligand
BARG347electrostatic stabiliser
BGLU366metal ligand
BARG368electrostatic stabiliser

site_idMCSA3
Number of Residues9
DetailsM-CSA 537
ChainResidueDetails
CASP54activator, proton acceptor
CGLU133metal ligand
CGLU135metal ligand
CGLU219metal ligand
CGLU227metal ligand
CHIS276metal ligand
CARG347electrostatic stabiliser
CGLU366metal ligand
CARG368electrostatic stabiliser

site_idMCSA4
Number of Residues9
DetailsM-CSA 537
ChainResidueDetails
DASP54activator, proton acceptor
DGLU133metal ligand
DGLU135metal ligand
DGLU219metal ligand
DGLU227metal ligand
DHIS276metal ligand
DARG347electrostatic stabiliser
DGLU366metal ligand
DARG368electrostatic stabiliser

site_idMCSA5
Number of Residues9
DetailsM-CSA 537
ChainResidueDetails
EASP54activator, proton acceptor
EGLU133metal ligand
EGLU135metal ligand
EGLU219metal ligand
EGLU227metal ligand
EHIS276metal ligand
EARG347electrostatic stabiliser
EGLU366metal ligand
EARG368electrostatic stabiliser

site_idMCSA6
Number of Residues9
DetailsM-CSA 537
ChainResidueDetails
FASP54activator, proton acceptor
FGLU133metal ligand
FGLU135metal ligand
FGLU219metal ligand
FGLU227metal ligand
FHIS276metal ligand
FARG347electrostatic stabiliser
FGLU366metal ligand
FARG368electrostatic stabiliser

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon