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	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
G	0000166	molecular_function	nucleotide binding
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	0005525	molecular_function	GTP 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	0019003	molecular_function	GDP binding
G	0019740	biological_process	nitrogen utilization
G	0030145	molecular_function	manganese ion binding
G	0035375	molecular_function	zymogen binding
G	0043531	molecular_function	ADP binding
G	0046872	molecular_function	metal ion binding
G	0050897	molecular_function	cobalt ion binding
G	0051260	biological_process	protein homooligomerization
H	0000166	molecular_function	nucleotide binding
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	0005525	molecular_function	GTP 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	0019003	molecular_function	GDP binding
H	0019740	biological_process	nitrogen utilization
H	0030145	molecular_function	manganese ion binding
H	0035375	molecular_function	zymogen binding
H	0043531	molecular_function	ADP binding
H	0046872	molecular_function	metal ion binding
H	0050897	molecular_function	cobalt ion binding
H	0051260	biological_process	protein homooligomerization
I	0000166	molecular_function	nucleotide binding
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	0005525	molecular_function	GTP 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	0019003	molecular_function	GDP binding
I	0019740	biological_process	nitrogen utilization
I	0030145	molecular_function	manganese ion binding
I	0035375	molecular_function	zymogen binding
I	0043531	molecular_function	ADP binding
I	0046872	molecular_function	metal ion binding
I	0050897	molecular_function	cobalt ion binding
I	0051260	biological_process	protein homooligomerization
J	0000166	molecular_function	nucleotide binding
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	0005525	molecular_function	GTP 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	0019003	molecular_function	GDP binding
J	0019740	biological_process	nitrogen utilization
J	0030145	molecular_function	manganese ion binding
J	0035375	molecular_function	zymogen binding
J	0043531	molecular_function	ADP binding
J	0046872	molecular_function	metal ion binding
J	0050897	molecular_function	cobalt ion binding
J	0051260	biological_process	protein homooligomerization
K	0000166	molecular_function	nucleotide binding
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	0005525	molecular_function	GTP 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	0019003	molecular_function	GDP binding
K	0019740	biological_process	nitrogen utilization
K	0030145	molecular_function	manganese ion binding
K	0035375	molecular_function	zymogen binding
K	0043531	molecular_function	ADP binding
K	0046872	molecular_function	metal ion binding
K	0050897	molecular_function	cobalt ion binding
K	0051260	biological_process	protein homooligomerization
L	0000166	molecular_function	nucleotide binding
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	0005525	molecular_function	GTP 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	0019003	molecular_function	GDP binding
L	0019740	biological_process	nitrogen utilization
L	0030145	molecular_function	manganese ion binding
L	0035375	molecular_function	zymogen binding
L	0043531	molecular_function	ADP binding
L	0046872	molecular_function	metal ion binding
L	0050897	molecular_function	cobalt 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 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_FI2
Number of Residues	36
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_FI3
Number of Residues	72
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_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P12425","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P77961","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A1P6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	12
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

---

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

---