Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4LNK

B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of GS-glutamate-AMPPCP complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0004356	molecular_function	glutamine synthetase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006542	biological_process	glutamine biosynthetic process
A	0016595	molecular_function	glutamate binding
A	0016874	molecular_function	ligase activity
A	0043562	biological_process	cellular response to nitrogen levels
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0046872	molecular_function	metal ion binding
A	0070406	molecular_function	glutamine binding
A	0090295	biological_process	nitrogen catabolite repression of transcription
A	0140297	molecular_function	DNA-binding transcription factor binding
A	1904797	biological_process	negative regulation of core promoter binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0004356	molecular_function	glutamine synthetase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006542	biological_process	glutamine biosynthetic process
B	0016595	molecular_function	glutamate binding
B	0016874	molecular_function	ligase activity
B	0043562	biological_process	cellular response to nitrogen levels
B	0045892	biological_process	negative regulation of DNA-templated transcription
B	0046872	molecular_function	metal ion binding
B	0070406	molecular_function	glutamine binding
B	0090295	biological_process	nitrogen catabolite repression of transcription
B	0140297	molecular_function	DNA-binding transcription factor binding
B	1904797	biological_process	negative regulation of core promoter binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0004356	molecular_function	glutamine synthetase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006542	biological_process	glutamine biosynthetic process
C	0016595	molecular_function	glutamate binding
C	0016874	molecular_function	ligase activity
C	0043562	biological_process	cellular response to nitrogen levels
C	0045892	biological_process	negative regulation of DNA-templated transcription
C	0046872	molecular_function	metal ion binding
C	0070406	molecular_function	glutamine binding
C	0090295	biological_process	nitrogen catabolite repression of transcription
C	0140297	molecular_function	DNA-binding transcription factor binding
C	1904797	biological_process	negative regulation of core promoter binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0004356	molecular_function	glutamine synthetase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006542	biological_process	glutamine biosynthetic process
D	0016595	molecular_function	glutamate binding
D	0016874	molecular_function	ligase activity
D	0043562	biological_process	cellular response to nitrogen levels
D	0045892	biological_process	negative regulation of DNA-templated transcription
D	0046872	molecular_function	metal ion binding
D	0070406	molecular_function	glutamine binding
D	0090295	biological_process	nitrogen catabolite repression of transcription
D	0140297	molecular_function	DNA-binding transcription factor binding
D	1904797	biological_process	negative regulation of core promoter binding
E	0000287	molecular_function	magnesium ion binding
E	0003824	molecular_function	catalytic activity
E	0004356	molecular_function	glutamine synthetase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0006542	biological_process	glutamine biosynthetic process
E	0016595	molecular_function	glutamate binding
E	0016874	molecular_function	ligase activity
E	0043562	biological_process	cellular response to nitrogen levels
E	0045892	biological_process	negative regulation of DNA-templated transcription
E	0046872	molecular_function	metal ion binding
E	0070406	molecular_function	glutamine binding
E	0090295	biological_process	nitrogen catabolite repression of transcription
E	0140297	molecular_function	DNA-binding transcription factor binding
E	1904797	biological_process	negative regulation of core promoter binding
F	0000287	molecular_function	magnesium ion binding
F	0003824	molecular_function	catalytic activity
F	0004356	molecular_function	glutamine synthetase activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0006542	biological_process	glutamine biosynthetic process
F	0016595	molecular_function	glutamate binding
F	0016874	molecular_function	ligase activity
F	0043562	biological_process	cellular response to nitrogen levels
F	0045892	biological_process	negative regulation of DNA-templated transcription
F	0046872	molecular_function	metal ion binding
F	0070406	molecular_function	glutamine binding
F	0090295	biological_process	nitrogen catabolite repression of transcription
F	0140297	molecular_function	DNA-binding transcription factor binding
F	1904797	biological_process	negative regulation of core promoter binding

Functional Information from PDB Data

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

Chain	Residue
A	GLU134
A	ARG335
A	MG504
A	GLU189
A	VAL190
A	ASN240
A	GLY241
A	GLY243
A	HIS245
A	ARG298
A	GLU304

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ADP A 502

Chain	Residue
A	GLY130
A	PHE199
A	TYR201
A	ASN247
A	SER249
A	SER325
A	ILE328
A	SER329
A	ARG331
B	LYS44
B	MET51

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 503

Chain	Residue
A	GLU132
A	HIS245
A	GLU333
B	GLU65

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 504

Chain	Residue
A	GLU134
A	GLU189
A	GLU196
A	GLU501

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 505

Chain	Residue
A	ASN48
A	LYS49
A	TYR69
A	TYR71

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 506

Chain	Residue
A	ASP73
A	ASN75
A	THR76
A	ARG206
A	ASP209
A	HOH607

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GLU B 501

Chain	Residue
B	GLU134
B	GLU189
B	ASN240
B	HIS245
B	ARG298
B	GLU304
B	ARG335
B	MG503
C	ARG62

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ADP B 502

Chain	Residue
B	GLY130
B	PHE199
B	TYR201
B	ASN247
B	SER249
B	SER325
B	ILE328
B	SER329
B	THR330
B	ARG331
C	LYS44
C	MET51

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 503

Chain	Residue
B	GLU134
B	GLU189
B	GLU196
B	HIS245
B	GLU501

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 504

Chain	Residue
B	GLU132
B	HIS245
B	GLU333
C	GLU65

site_id	BC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE GLU C 501

Chain	Residue
C	GLU134
C	TYR156
C	GLU189
C	VAL190
C	GLN194
C	ASN240
C	GLY241
C	GLY243
C	HIS245
C	ARG298
C	GLU304
C	MG503
C	HOH604

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ADP C 502

Chain	Residue
C	GLY130
C	PHE199
C	TYR201
C	ASN247
C	SER249
C	SER325
C	ILE328
C	SER329
C	ARG331
D	LYS44
D	MET51

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 503

Chain	Residue
C	GLU134
C	GLU189
C	GLU196
C	GLU501

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 504

Chain	Residue
C	HIS245
C	GLU333
D	GLU65
C	GLU132

site_id	BC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GLU D 501

Chain	Residue
D	GLU134
D	TYR156
D	GLU189
D	ASN240
D	GLY241
D	GLY243
D	HIS245
D	ARG298
D	TYR303
D	GLU304
D	ALA305
D	MG503

site_id	BC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ADP D 502

Chain	Residue
D	GLY130
D	GLU184
D	PHE199
D	TYR201
D	ASN247
D	SER249
D	SER325
D	ILE328
D	SER329
D	ARG331
E	LYS44
E	MET51

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 503

Chain	Residue
D	GLU134
D	HIS187
D	GLU189
D	GLU196
D	GLU501
E	HOH601

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 504

Chain	Residue
D	GLU132
D	HIS245
D	GLU333
E	GLU65
E	HOH601

site_id	CC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GLU E 501

Chain	Residue
E	GLU134
E	GLU189
E	ASN240
E	GLY241
E	GLY243
E	HIS245
E	ARG298
E	GLU304
E	PRO306
E	ARG335
E	MG504

site_id	CC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ADP E 502

Chain	Residue
E	ASN128
E	GLY130
E	PHE199
E	TYR201
E	ASN247
E	SER249
E	PHE251
E	SER325
E	ILE328
E	SER329
E	ARG331
F	LYS44
F	LYS49
F	MET51

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 503

Chain	Residue
E	GLU132
E	HIS245
E	GLU333
F	GLU65

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 504

Chain	Residue
E	GLU132
E	GLU134
E	GLU189
E	GLU196
E	GLU501

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 505

Chain	Residue
E	ASN17
E	THR83
E	ALA84
E	LYS86
E	GLY87
E	LYS88

site_id	CC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GLU F 501

Chain	Residue
A	ARG62
F	GLU134
F	GLU189
F	VAL190
F	ASN240
F	GLY241
F	HIS245
F	ARG298
F	GLU304

site_id	CC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ADP F 502

Chain	Residue
A	LYS44
A	MET51
F	GLY130
F	GLU184
F	PHE199
F	TYR201
F	ASN247
F	SER249
F	SER325
F	ILE328
F	SER329
F	ARG331

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG F 503

Chain	Residue
F	GLU132
F	HIS245
F	GLU333

site_id	CC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG F 504

Chain	Residue
F	GLU134
F	GLU189
F	GLU196

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE52-LEU70

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

Chain	Residue	Details
A	LYS234-SER249

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

Chain	Residue	Details
A	LYS361-TYR373

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:24158439, ECO:0000269\|PubMed:25691471, ECO:0007744\|PDB:4LNF, ECO:0007744\|PDB:4LNI, ECO:0007744\|PDB:4LNK, ECO:0007744\|PDB:4LNN, ECO:0007744\|PDB:4S0R

Chain	Residue	Details
A	GLU132
E	GLU333
F	GLU132
F	GLU333
A	GLU333
B	GLU132
B	GLU333
C	GLU132
C	GLU333
D	GLU132
D	GLU333
E	GLU132

site_id	SWS_FT_FI2
Number of Residues	18
Details	BINDING: BINDING => ECO:0000269\|PubMed:24158439, ECO:0000269\|PubMed:25691471, ECO:0007744\|PDB:4LNF, ECO:0007744\|PDB:4LNI, ECO:0007744\|PDB:4LNK, ECO:0007744\|PDB:4S0R

Chain	Residue	Details
A	GLU134
D	GLU134
D	GLU189
D	GLU196
E	GLU134
E	GLU189
E	GLU196
F	GLU134
F	GLU189
F	GLU196
A	GLU189
A	GLU196
B	GLU134
B	GLU189
B	GLU196
C	GLU134
C	GLU189
C	GLU196

site_id	SWS_FT_FI3
Number of Residues	24
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P9WN39

Chain	Residue	Details
A	GLU184
C	ASN240
C	ARG316
C	ARG321
D	GLU184
D	ASN240
D	ARG316
D	ARG321
E	GLU184
E	ASN240
E	ARG316
A	ASN240
E	ARG321
F	GLU184
F	ASN240
F	ARG316
F	ARG321
A	ARG316
A	ARG321
B	GLU184
B	ASN240
B	ARG316
B	ARG321
C	GLU184

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:24158439, ECO:0000269\|PubMed:25691471, ECO:0007744\|PDB:4LNF, ECO:0007744\|PDB:4LNK, ECO:0007744\|PDB:4LNN, ECO:0007744\|PDB:4S0R

Chain	Residue	Details
A	GLY241
B	GLY241
C	GLY241
D	GLY241
E	GLY241
F	GLY241

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:24158439, ECO:0000269\|PubMed:25691471, ECO:0007744\|PDB:4LNF, ECO:0007744\|PDB:4LNK, ECO:0007744\|PDB:4S0R

Chain	Residue	Details
A	HIS245
B	HIS245
C	HIS245
D	HIS245
E	HIS245
F	HIS245

site_id	SWS_FT_FI6
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P77961

Chain	Residue	Details
A	SER249
B	SER249
C	SER249
D	SER249
E	SER249
F	SER249

site_id	SWS_FT_FI7
Number of Residues	18
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P0A1P6

Chain	Residue	Details
A	ARG298
D	ARG298
D	GLU304
D	ARG335
E	ARG298
E	GLU304
E	ARG335
F	ARG298
F	GLU304
F	ARG335
A	GLU304
A	ARG335
B	ARG298
B	GLU304
B	ARG335
C	ARG298
C	GLU304
C	ARG335

site_id	SWS_FT_FI8
Number of Residues	6
Details	SITE: Important for inhibition by glutamine => ECO:0000269\|PubMed:24158439

Chain	Residue	Details
A	ARG62
B	ARG62
C	ARG62
D	ARG62
E	ARG62
F	ARG62

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