Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2GLS

REFINED ATOMIC MODEL OF GLUTAMINE SYNTHETASE AT 3.5 ANGSTROMS RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0004356	molecular_function	glutamine synthetase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006541	biological_process	glutamine metabolic process
A	0006542	biological_process	glutamine biosynthetic process
A	0016020	cellular_component	membrane
A	0016874	molecular_function	ligase activity
A	0019740	biological_process	nitrogen utilization
A	0030145	molecular_function	manganese ion binding
A	0046872	molecular_function	metal ion binding
A	0051260	biological_process	protein homooligomerization
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0004356	molecular_function	glutamine synthetase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006541	biological_process	glutamine metabolic process
B	0006542	biological_process	glutamine biosynthetic process
B	0016020	cellular_component	membrane
B	0016874	molecular_function	ligase activity
B	0019740	biological_process	nitrogen utilization
B	0030145	molecular_function	manganese ion binding
B	0046872	molecular_function	metal ion binding
B	0051260	biological_process	protein homooligomerization
C	0000166	molecular_function	nucleotide binding
C	0003824	molecular_function	catalytic activity
C	0004356	molecular_function	glutamine synthetase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006541	biological_process	glutamine metabolic process
C	0006542	biological_process	glutamine biosynthetic process
C	0016020	cellular_component	membrane
C	0016874	molecular_function	ligase activity
C	0019740	biological_process	nitrogen utilization
C	0030145	molecular_function	manganese ion binding
C	0046872	molecular_function	metal ion binding
C	0051260	biological_process	protein homooligomerization
D	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
D	0004356	molecular_function	glutamine synthetase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006541	biological_process	glutamine metabolic process
D	0006542	biological_process	glutamine biosynthetic process
D	0016020	cellular_component	membrane
D	0016874	molecular_function	ligase activity
D	0019740	biological_process	nitrogen utilization
D	0030145	molecular_function	manganese ion binding
D	0046872	molecular_function	metal ion binding
D	0051260	biological_process	protein homooligomerization
E	0000166	molecular_function	nucleotide binding
E	0003824	molecular_function	catalytic activity
E	0004356	molecular_function	glutamine synthetase activity
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0006541	biological_process	glutamine metabolic process
E	0006542	biological_process	glutamine biosynthetic process
E	0016020	cellular_component	membrane
E	0016874	molecular_function	ligase activity
E	0019740	biological_process	nitrogen utilization
E	0030145	molecular_function	manganese ion binding
E	0046872	molecular_function	metal ion binding
E	0051260	biological_process	protein homooligomerization
F	0000166	molecular_function	nucleotide binding
F	0003824	molecular_function	catalytic activity
F	0004356	molecular_function	glutamine synthetase activity
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0006541	biological_process	glutamine metabolic process
F	0006542	biological_process	glutamine biosynthetic process
F	0016020	cellular_component	membrane
F	0016874	molecular_function	ligase activity
F	0019740	biological_process	nitrogen utilization
F	0030145	molecular_function	manganese ion binding
F	0046872	molecular_function	metal ion binding
F	0051260	biological_process	protein homooligomerization
G	0000166	molecular_function	nucleotide binding
G	0003824	molecular_function	catalytic activity
G	0004356	molecular_function	glutamine synthetase activity
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0006541	biological_process	glutamine metabolic process
G	0006542	biological_process	glutamine biosynthetic process
G	0016020	cellular_component	membrane
G	0016874	molecular_function	ligase activity
G	0019740	biological_process	nitrogen utilization
G	0030145	molecular_function	manganese ion binding
G	0046872	molecular_function	metal ion binding
G	0051260	biological_process	protein homooligomerization
H	0000166	molecular_function	nucleotide binding
H	0003824	molecular_function	catalytic activity
H	0004356	molecular_function	glutamine synthetase activity
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0006541	biological_process	glutamine metabolic process
H	0006542	biological_process	glutamine biosynthetic process
H	0016020	cellular_component	membrane
H	0016874	molecular_function	ligase activity
H	0019740	biological_process	nitrogen utilization
H	0030145	molecular_function	manganese ion binding
H	0046872	molecular_function	metal ion binding
H	0051260	biological_process	protein homooligomerization
I	0000166	molecular_function	nucleotide binding
I	0003824	molecular_function	catalytic activity
I	0004356	molecular_function	glutamine synthetase activity
I	0005524	molecular_function	ATP binding
I	0005737	cellular_component	cytoplasm
I	0006541	biological_process	glutamine metabolic process
I	0006542	biological_process	glutamine biosynthetic process
I	0016020	cellular_component	membrane
I	0016874	molecular_function	ligase activity
I	0019740	biological_process	nitrogen utilization
I	0030145	molecular_function	manganese ion binding
I	0046872	molecular_function	metal ion binding
I	0051260	biological_process	protein homooligomerization
J	0000166	molecular_function	nucleotide binding
J	0003824	molecular_function	catalytic activity
J	0004356	molecular_function	glutamine synthetase activity
J	0005524	molecular_function	ATP binding
J	0005737	cellular_component	cytoplasm
J	0006541	biological_process	glutamine metabolic process
J	0006542	biological_process	glutamine biosynthetic process
J	0016020	cellular_component	membrane
J	0016874	molecular_function	ligase activity
J	0019740	biological_process	nitrogen utilization
J	0030145	molecular_function	manganese ion binding
J	0046872	molecular_function	metal ion binding
J	0051260	biological_process	protein homooligomerization
K	0000166	molecular_function	nucleotide binding
K	0003824	molecular_function	catalytic activity
K	0004356	molecular_function	glutamine synthetase activity
K	0005524	molecular_function	ATP binding
K	0005737	cellular_component	cytoplasm
K	0006541	biological_process	glutamine metabolic process
K	0006542	biological_process	glutamine biosynthetic process
K	0016020	cellular_component	membrane
K	0016874	molecular_function	ligase activity
K	0019740	biological_process	nitrogen utilization
K	0030145	molecular_function	manganese ion binding
K	0046872	molecular_function	metal ion binding
K	0051260	biological_process	protein homooligomerization
L	0000166	molecular_function	nucleotide binding
L	0003824	molecular_function	catalytic activity
L	0004356	molecular_function	glutamine synthetase activity
L	0005524	molecular_function	ATP binding
L	0005737	cellular_component	cytoplasm
L	0006541	biological_process	glutamine metabolic process
L	0006542	biological_process	glutamine biosynthetic process
L	0016020	cellular_component	membrane
L	0016874	molecular_function	ligase activity
L	0019740	biological_process	nitrogen utilization
L	0030145	molecular_function	manganese ion binding
L	0046872	molecular_function	metal ion binding
L	0051260	biological_process	protein homooligomerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 469

Chain	Residue
A	GLU131
A	GLU212
A	GLU220
A	HOH471

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 470

Chain	Residue
A	GLU129
A	HIS269
A	GLU357
A	HOH472

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN B 469

Chain	Residue
B	GLU212
B	GLU220
B	HOH471
B	GLU131

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN B 470

Chain	Residue
B	GLU129
B	HIS269
B	GLU357
B	HOH472

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN C 469

Chain	Residue
C	GLU131
C	GLU212
C	GLU220
C	HOH471

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN C 470

Chain	Residue
C	GLU129
C	HIS269
C	GLU357
C	HOH472

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN D 469

Chain	Residue
D	GLU131
D	GLU212
D	GLU220
D	HOH471

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN D 470

Chain	Residue
D	GLU129
D	HIS269
D	GLU357
D	HOH472

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN E 469

Chain	Residue
E	GLU131
E	GLU212
E	GLU220
E	HOH471

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN E 470

Chain	Residue
E	GLU129
E	HIS269
E	GLU357
E	HOH472

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN F 469

Chain	Residue
F	GLU131
F	GLU212
F	GLU220
F	HOH471

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN F 470

Chain	Residue
F	GLU129
F	HIS269
F	GLU357
F	HOH472

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN G 469

Chain	Residue
G	GLU131
G	GLU212
G	GLU220
G	HOH471

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN G 470

Chain	Residue
G	GLU129
G	HIS269
G	GLU357
G	HOH472

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN H 469

Chain	Residue
H	GLU131
H	GLU212
H	GLU220
H	HOH471

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN H 470

Chain	Residue
H	GLU129
H	HIS269
H	GLU357
H	HOH472

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN I 469

Chain	Residue
I	GLU131
I	GLU212
I	GLU220
I	HOH471

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN I 470

Chain	Residue
I	GLU129
I	HIS269
I	GLU357
I	HOH472

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN J 469

Chain	Residue
J	GLU131
J	GLU212
J	GLU220
J	HOH471

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN J 470

Chain	Residue
J	GLU129
J	HIS269
J	GLU357
J	HOH472

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN K 469

Chain	Residue
K	GLU131
K	GLU212
K	GLU220
K	HOH471

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN K 470

Chain	Residue
K	GLU129
K	HIS269
K	GLU357
K	HOH472

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN L 469

Chain	Residue
L	GLU131
L	GLU212
L	GLU220
L	HOH471

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN L 470

Chain	Residue
L	GLU129
L	HIS269
L	GLU357
L	HOH472

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE49-LEU67

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

Chain	Residue	Details
A	LYS258-SER273

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

Chain	Residue	Details
A	LYS385-TYR397

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1008
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	4368
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	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11329256","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2572586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8099447","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FPY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GLS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LGS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11329256","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7727369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8099447","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FPY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LGR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LGS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7727369","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LGR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7727369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8099447","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11329256","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1F1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FPY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LGR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LGS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P12425","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11329256","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FPY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P77961","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8099447","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11329256","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1FPY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LGS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11329256","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1FPY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P9WN39","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11329256","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2572586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7727369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8099447","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FPY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LGR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GLS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LGS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8099447","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2LGS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	12
Details	Modified residue: {"description":"O-AMP-tyrosine","evidences":[{"source":"UniProtKB","id":"P9WN39","evidenceCode":"ECO:0000250"}]}

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	ARG339
A	ASP50
A	GLU327

site_id	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1hto

Chain	Residue	Details
J	ARG339
J	ASP50
J	GLU327

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1hto

Chain	Residue	Details
K	ARG339
K	ASP50
K	GLU327

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1hto

Chain	Residue	Details
L	ARG339
L	ASP50
L	GLU327

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

Chain	Residue	Details
B	ARG339
B	ASP50
B	GLU327

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

Chain	Residue	Details
C	ARG339
C	ASP50
C	GLU327

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

Chain	Residue	Details
D	ARG339
D	ASP50
D	GLU327

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

Chain	Residue	Details
E	ARG339
E	ASP50
E	GLU327

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

Chain	Residue	Details
F	ARG339
F	ASP50
F	GLU327

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1hto

Chain	Residue	Details
G	ARG339
G	ASP50
G	GLU327

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1hto

Chain	Residue	Details
H	ARG339
H	ASP50
H	GLU327

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1hto

Chain	Residue	Details
I	ARG339
I	ASP50
I	GLU327

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)