Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2WHI

Crystal structure of Mycobacterium Tuberculosis Glutamine Synthetase in complex with a purine analogue inhibitor and L-methionine-S- sulfoximine phosphate.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0001968	molecular_function	fibronectin binding
A	0003824	molecular_function	catalytic activity
A	0004356	molecular_function	glutamine synthetase activity
A	0005524	molecular_function	ATP binding
A	0005525	molecular_function	GTP 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	0019003	molecular_function	GDP binding
A	0019740	biological_process	nitrogen utilization
A	0030145	molecular_function	manganese ion binding
A	0035375	molecular_function	zymogen binding
A	0043531	molecular_function	ADP binding
A	0046872	molecular_function	metal ion binding
A	0050897	molecular_function	cobalt ion binding
A	0051260	biological_process	protein homooligomerization
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0001968	molecular_function	fibronectin binding
B	0003824	molecular_function	catalytic activity
B	0004356	molecular_function	glutamine synthetase activity
B	0005524	molecular_function	ATP binding
B	0005525	molecular_function	GTP 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	0019003	molecular_function	GDP binding
B	0019740	biological_process	nitrogen utilization
B	0030145	molecular_function	manganese ion binding
B	0035375	molecular_function	zymogen binding
B	0043531	molecular_function	ADP binding
B	0046872	molecular_function	metal ion binding
B	0050897	molecular_function	cobalt ion binding
B	0051260	biological_process	protein homooligomerization
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0001968	molecular_function	fibronectin binding
C	0003824	molecular_function	catalytic activity
C	0004356	molecular_function	glutamine synthetase activity
C	0005524	molecular_function	ATP binding
C	0005525	molecular_function	GTP 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	0019003	molecular_function	GDP binding
C	0019740	biological_process	nitrogen utilization
C	0030145	molecular_function	manganese ion binding
C	0035375	molecular_function	zymogen binding
C	0043531	molecular_function	ADP binding
C	0046872	molecular_function	metal ion binding
C	0050897	molecular_function	cobalt ion binding
C	0051260	biological_process	protein homooligomerization
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0001968	molecular_function	fibronectin binding
D	0003824	molecular_function	catalytic activity
D	0004356	molecular_function	glutamine synthetase activity
D	0005524	molecular_function	ATP binding
D	0005525	molecular_function	GTP 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	0019003	molecular_function	GDP binding
D	0019740	biological_process	nitrogen utilization
D	0030145	molecular_function	manganese ion binding
D	0035375	molecular_function	zymogen binding
D	0043531	molecular_function	ADP binding
D	0046872	molecular_function	metal ion binding
D	0050897	molecular_function	cobalt ion binding
D	0051260	biological_process	protein homooligomerization
E	0000166	molecular_function	nucleotide binding
E	0000287	molecular_function	magnesium ion binding
E	0001968	molecular_function	fibronectin binding
E	0003824	molecular_function	catalytic activity
E	0004356	molecular_function	glutamine synthetase activity
E	0005524	molecular_function	ATP binding
E	0005525	molecular_function	GTP 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	0019003	molecular_function	GDP binding
E	0019740	biological_process	nitrogen utilization
E	0030145	molecular_function	manganese ion binding
E	0035375	molecular_function	zymogen binding
E	0043531	molecular_function	ADP binding
E	0046872	molecular_function	metal ion binding
E	0050897	molecular_function	cobalt ion binding
E	0051260	biological_process	protein homooligomerization
F	0000166	molecular_function	nucleotide binding
F	0000287	molecular_function	magnesium ion binding
F	0001968	molecular_function	fibronectin binding
F	0003824	molecular_function	catalytic activity
F	0004356	molecular_function	glutamine synthetase activity
F	0005524	molecular_function	ATP binding
F	0005525	molecular_function	GTP 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	0019003	molecular_function	GDP binding
F	0019740	biological_process	nitrogen utilization
F	0030145	molecular_function	manganese ion binding
F	0035375	molecular_function	zymogen binding
F	0043531	molecular_function	ADP binding
F	0046872	molecular_function	metal ion binding
F	0050897	molecular_function	cobalt ion binding
F	0051260	biological_process	protein homooligomerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 1AZ A 501

Chain	Residue
A	TYR129
A	PO4506
A	HOH2153
A	GLY131
A	TYR230
A	PHE232
A	HIS278
A	SER280
A	TRP282
A	LYS361
A	ARG364

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 502

Chain	Residue
A	GLU135
A	GLU219
A	GLU227
A	P3S505
A	HOH2159

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 503

Chain	Residue
A	GLU133
A	HIS276
A	GLU366
A	P3S505
A	PO4506

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 504

Chain	Residue
A	GLU133
A	GLU227
A	P3S505
A	PO4506
A	HOH2156
A	HOH2161

site_id	AC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE P3S A 505

Chain	Residue
A	GLU133
A	GLU135
A	GLU219
A	GLU227
A	GLY272
A	HIS276
A	ARG329
A	GLU335
A	ARG347
A	GLU366
A	ARG368
A	MG502
A	MG503
A	MG504
A	PO4506
A	HOH2125
A	HOH2156
A	HOH2157
A	HOH2159
A	HOH2273
F	ASP54

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 A 506

Chain	Residue
A	GLU133
A	HIS278
A	ARG347
A	ARG352
A	GLU366
A	1AZ501
A	MG503
A	MG504
A	P3S505
A	HOH2161
A	HOH2274

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 507

Chain	Residue
A	SER424

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 1PE A 508

Chain	Residue
A	SER56
A	SER57
A	ARG59
A	HOH2276
B	LYS183
B	HOH2118
E	LEU474

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 1AZ B 501

Chain	Residue
B	TYR129
B	GLY131
B	TYR230
B	PHE232
B	HIS278
B	SER280
B	TRP282
B	LYS361
B	ARG364
B	PO4506
B	HOH2152

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 502

Chain	Residue
B	GLU135
B	GLU219
B	GLU227
B	P3S505
B	HOH2274

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 503

Chain	Residue
B	GLU133
B	HIS276
B	GLU366
B	P3S505
B	PO4506

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 504

Chain	Residue
B	GLU133
B	GLU227
B	P3S505
B	PO4506
B	HOH2155
B	HOH2160

site_id	BC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE P3S B 505

Chain	Residue
B	GLY272
B	HIS276
B	ARG329
B	GLU335
B	ARG347
B	GLU366
B	ARG368
B	MG502
B	MG503
B	MG504
B	PO4506
B	HOH2123
B	HOH2157
B	HOH2273
B	HOH2274
A	ASP54
B	GLU133
B	GLU135
B	GLU219
B	GLU227

site_id	BC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PO4 B 506

Chain	Residue
B	GLU133
B	HIS278
B	ARG347
B	ARG352
B	GLU366
B	1AZ501
B	MG503
B	MG504
B	P3S505
B	HOH2160
B	HOH2275
B	HOH2276

site_id	BC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL B 507

Chain	Residue
B	SER424

site_id	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 1PE B 508

Chain	Residue
B	SER56
B	SER57
B	ARG59
B	PHE454
B	HOH2277
C	LYS183
C	HOH2116
D	LEU474

site_id	BC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 1AZ C 501

Chain	Residue
C	TYR129
C	GLY131
C	TYR230
C	PHE232
C	HIS278
C	SER280
C	TRP282
C	LYS361
C	ARG364
C	PO4506
C	HOH2151

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 502

Chain	Residue
C	GLU135
C	GLU219
C	GLU227
C	P3S505
C	HOH2157

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 503

Chain	Residue
C	GLU133
C	HIS276
C	GLU366
C	ARG368
C	P3S505
C	PO4506

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 504

Chain	Residue
C	GLU133
C	GLU227
C	P3S505
C	PO4506
C	HOH2154
C	HOH2159

site_id	CC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE P3S C 505

Chain	Residue
B	ASP54
C	GLU133
C	GLU135
C	GLU219
C	GLU227
C	GLY272
C	HIS276
C	ARG329
C	GLU335
C	ARG347
C	GLU366
C	ARG368
C	MG502
C	MG503
C	MG504
C	PO4506
C	HOH2121
C	HOH2154
C	HOH2155
C	HOH2157
C	HOH2271

site_id	CC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PO4 C 506

Chain	Residue
C	GLU133
C	HIS278
C	ARG347
C	ARG352
C	GLU366
C	1AZ501
C	MG503
C	MG504
C	P3S505
C	HOH2154
C	HOH2159
C	HOH2273

site_id	CC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL C 507

Chain	Residue
C	SER424

site_id	CC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 1PE C 508

Chain	Residue
C	SER56
C	SER57
C	ARG59
C	PHE454
C	GLU459
C	LEU474
C	HOH2274
D	LYS183

site_id	CC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 1AZ D 501

Chain	Residue
D	TYR129
D	GLY131
D	TYR230
D	PHE232
D	HIS278
D	SER280
D	TRP282
D	LYS361
D	ARG364
D	PO4506
D	HOH2151

site_id	CC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 502

Chain	Residue
D	GLU135
D	GLU219
D	GLU227
D	P3S505
D	HOH2275

site_id	CC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 503

Chain	Residue
D	GLU133
D	HIS276
D	GLU366
D	P3S505
D	PO4506

site_id	DC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 504

Chain	Residue
D	GLU133
D	GLU227
D	P3S505
D	PO4506
D	HOH2154
D	HOH2159

site_id	DC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE P3S D 505

Chain	Residue
C	ASP54
D	GLU133
D	GLU135
D	GLU219
D	GLU227
D	GLY272
D	HIS276
D	ARG329
D	GLU335
D	ARG347
D	GLU366
D	ARG368
D	MG502
D	MG503
D	MG504
D	PO4506
D	HOH2123
D	HOH2156
D	HOH2275
D	HOH2276

site_id	DC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 D 506

Chain	Residue
D	GLU133
D	HIS278
D	ARG347
D	ARG352
D	GLU366
D	1AZ501
D	MG503
D	MG504
D	P3S505
D	HOH2159
D	HOH2278

site_id	DC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL D 507

Chain	Residue
D	SER424

site_id	DC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 1PE D 508

Chain	Residue
B	LEU474
D	SER56
D	SER57
D	ARG59
D	HOH2279
E	LYS183

site_id	DC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 1AZ E 501

Chain	Residue
E	TYR129
E	GLY131
E	TYR230
E	PHE232
E	HIS278
E	SER280
E	TRP282
E	LYS361
E	ARG364
E	PO4506
E	HOH2150

site_id	DC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 502

Chain	Residue
E	GLU135
E	GLU219
E	GLU227
E	P3S505
E	HOH2271

site_id	DC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 503

Chain	Residue
E	GLU133
E	HIS276
E	GLU366
E	P3S505
E	PO4506

site_id	DC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG E 504

Chain	Residue
E	GLU133
E	GLU227
E	P3S505
E	PO4506
E	HOH2152
E	HOH2156

site_id	EC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE P3S E 505

Chain	Residue
D	ASP54
E	GLU133
E	GLU135
E	GLU219
E	GLU227
E	GLY272
E	HIS276
E	ARG329
E	GLU335
E	ARG347
E	GLU366
E	ARG368
E	MG502
E	MG503
E	MG504
E	PO4506
E	HOH2121
E	HOH2152
E	HOH2153
E	HOH2271
E	HOH2272

site_id	EC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 E 506

Chain	Residue
E	GLU133
E	HIS278
E	ARG347
E	ARG352
E	GLU366
E	1AZ501
E	MG503
E	MG504
E	P3S505
E	HOH2156
E	HOH2274

site_id	EC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL E 507

Chain	Residue
E	SER424

site_id	EC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 1PE E 508

Chain	Residue
A	LEU474
E	SER56
E	SER57
E	ARG59
E	HOH2275
F	LYS183

site_id	EC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 1AZ F 501

Chain	Residue
F	TYR129
F	GLY131
F	TYR230
F	PHE232
F	HIS278
F	SER280
F	TRP282
F	LYS361
F	ARG364
F	PO4506
F	HOH2148

site_id	EC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 502

Chain	Residue
F	GLU135
F	GLU219
F	GLU227
F	P3S505
F	HOH2067

site_id	EC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 503

Chain	Residue
F	GLU133
F	HIS276
F	GLU366
F	P3S505
F	PO4506

site_id	EC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG F 504

Chain	Residue
F	GLU133
F	GLU227
F	P3S505
F	PO4506
F	HOH2150
F	HOH2154

site_id	EC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE P3S F 505

Chain	Residue
E	ASP54
F	GLU133
F	GLU135
F	GLU219
F	GLU227
F	GLY272
F	HIS276
F	ARG329
F	GLU335
F	ARG347
F	GLU366
F	ARG368
F	MG502
F	MG503
F	MG504
F	PO4506
F	HOH2067
F	HOH2121
F	HOH2150
F	HOH2151
F	HOH2266

site_id	FC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PO4 F 506

Chain	Residue
F	GLU133
F	HIS278
F	ARG347
F	ARG352
F	GLU366
F	1AZ501
F	MG503
F	MG504
F	P3S505
F	HOH2154
F	HOH2267
F	HOH2268

site_id	FC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL F 507

Chain	Residue
F	SER424

site_id	FC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 1PE F 508

Chain	Residue
A	LYS183
F	SER57
F	ARG59
F	GLU459
F	LEU474
F	HOH2269

Functional Information from PROSITE/UniProt

site_id	PS00180
Number of Residues	19
Details	GLNA_1 Glutamine synthetase signature 1. FDGSSirgfqsihESDmlL

Chain	Residue	Details
A	PHE53-LEU71

site_id	PS00181
Number of Residues	16
Details	GLNA_ATP Glutamine synthetase putative ATP-binding region signature. KPLfgd..NGSGmHchqS

Chain	Residue	Details
A	LYS265-SER280

site_id	PS00182
Number of Residues	13
Details	GLNA_ADENYLATION Glutamine synthetase class-I adenylation site. KIepqapVDKDLY

Chain	Residue	Details
A	LYS394-TYR406

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	504
Details	Domain: {"description":"GS beta-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU01330","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2220
Details	Domain: {"description":"GS catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU01331","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16027359","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19695264","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22369127","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2012","firstPage":"620","lastPage":"626","volume":"3","journal":"Med. Chem. Commun.","title":"Synthesis, biological evaluation and X-Ray crystallographic studies of imidazo(1,2-A)pyridine-based Mycobacterium tuberculosis glutamine synthetase inhibitors.","authors":["Nordqvist A.","Nilsson M.T.","Lagerlund O.","Muthas D.","Gising J.","Yahiaoui S.","Odell L.R.","Srinivasa B.R.","Larhed M.","Mowbray S.L.","Karlen A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/C2MD00310D"}]}},{"source":"PDB","id":"2BVC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WHI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZXR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZXV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ACF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16027359","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2BVC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16027359","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19695264","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22369127","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"journal article","publicationDate":"2012","firstPage":"620","lastPage":"626","volume":"3","journal":"Med. Chem. Commun.","title":"Synthesis, biological evaluation and X-Ray crystallographic studies of imidazo(1,2-A)pyridine-based Mycobacterium tuberculosis glutamine synthetase inhibitors.","authors":["Nordqvist A.","Nilsson M.T.","Lagerlund O.","Muthas D.","Gising J.","Yahiaoui S.","Odell L.R.","Srinivasa B.R.","Larhed M.","Mowbray S.L.","Karlen A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/C2MD00310D"}]}},{"source":"PDB","id":"2BVC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WHI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZXR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZXV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ACF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P12425","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P77961","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A1P6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16027359","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22369127","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"journal article","publicationDate":"2012","firstPage":"620","lastPage":"626","volume":"3","journal":"Med. Chem. Commun.","title":"Synthesis, biological evaluation and X-Ray crystallographic studies of imidazo(1,2-A)pyridine-based Mycobacterium tuberculosis glutamine synthetase inhibitors.","authors":["Nordqvist A.","Nilsson M.T.","Lagerlund O.","Muthas D.","Gising J.","Yahiaoui S.","Odell L.R.","Srinivasa B.R.","Larhed M.","Mowbray S.L.","Karlen A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/C2MD00310D"}]}},{"source":"PDB","id":"2BVC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZXR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZXV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ACF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	6
Details	Modified residue: {"description":"O-AMP-tyrosine","evidences":[{"source":"PubMed","id":"15037612","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12146952","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16027359","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1hto

Chain	Residue	Details
A	ASP54
A	ARG347
A	GLU335

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1hto

Chain	Residue	Details
B	ASP54
B	ARG347
B	GLU335

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1hto

Chain	Residue	Details
C	ASP54
C	ARG347
C	GLU335

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1hto

Chain	Residue	Details
D	ASP54
D	ARG347
D	GLU335

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1hto

Chain	Residue	Details
E	ASP54
E	ARG347
E	GLU335

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1hto

Chain	Residue	Details
F	ASP54
F	ARG347
F	GLU335

site_id	MCSA1
Number of Residues	9
Details	M-CSA 537

Chain	Residue	Details
A	ASP54	activator, proton acceptor
A	GLU133	metal ligand
A	GLU135	metal ligand
A	GLU219	metal ligand
A	GLU227	metal ligand
A	HIS276	metal ligand
A	ARG347	electrostatic stabiliser
A	GLU366	metal ligand
A	ARG368	electrostatic stabiliser

site_id	MCSA2
Number of Residues	9
Details	M-CSA 537

Chain	Residue	Details
B	ASP54	activator, proton acceptor
B	GLU133	metal ligand
B	GLU135	metal ligand
B	GLU219	metal ligand
B	GLU227	metal ligand
B	HIS276	metal ligand
B	ARG347	electrostatic stabiliser
B	GLU366	metal ligand
B	ARG368	electrostatic stabiliser

site_id	MCSA3
Number of Residues	9
Details	M-CSA 537

Chain	Residue	Details
C	ASP54	activator, proton acceptor
C	GLU133	metal ligand
C	GLU135	metal ligand
C	GLU219	metal ligand
C	GLU227	metal ligand
C	HIS276	metal ligand
C	ARG347	electrostatic stabiliser
C	GLU366	metal ligand
C	ARG368	electrostatic stabiliser

site_id	MCSA4
Number of Residues	9
Details	M-CSA 537

Chain	Residue	Details
D	ASP54	activator, proton acceptor
D	GLU133	metal ligand
D	GLU135	metal ligand
D	GLU219	metal ligand
D	GLU227	metal ligand
D	HIS276	metal ligand
D	ARG347	electrostatic stabiliser
D	GLU366	metal ligand
D	ARG368	electrostatic stabiliser

site_id	MCSA5
Number of Residues	9
Details	M-CSA 537

Chain	Residue	Details
E	ASP54	activator, proton acceptor
E	GLU133	metal ligand
E	GLU135	metal ligand
E	GLU219	metal ligand
E	GLU227	metal ligand
E	HIS276	metal ligand
E	ARG347	electrostatic stabiliser
E	GLU366	metal ligand
E	ARG368	electrostatic stabiliser

site_id	MCSA6
Number of Residues	9
Details	M-CSA 537

Chain	Residue	Details
F	ASP54	activator, proton acceptor
F	GLU133	metal ligand
F	GLU135	metal ligand
F	GLU219	metal ligand
F	GLU227	metal ligand
F	HIS276	metal ligand
F	ARG347	electrostatic stabiliser
F	GLU366	metal ligand
F	ARG368	electrostatic stabiliser

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)