Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6S6T

Structure of Azospirillum brasilense Glutamate Synthase in a4b3 oligomeric state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004355	molecular_function	glutamate synthase (NADPH) activity
A	0006537	biological_process	glutamate biosynthetic process
A	0008652	biological_process	amino acid biosynthetic process
A	0015930	molecular_function	glutamate synthase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
A	0019676	biological_process	ammonia assimilation cycle
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051538	molecular_function	3 iron, 4 sulfur cluster binding
A	0097054	biological_process	L-glutamate biosynthetic process
B	0004355	molecular_function	glutamate synthase (NADPH) activity
B	0006537	biological_process	glutamate biosynthetic process
B	0008652	biological_process	amino acid biosynthetic process
B	0015930	molecular_function	glutamate synthase activity
B	0016491	molecular_function	oxidoreductase activity
B	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
B	0019676	biological_process	ammonia assimilation cycle
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051538	molecular_function	3 iron, 4 sulfur cluster binding
B	0097054	biological_process	L-glutamate biosynthetic process
C	0004355	molecular_function	glutamate synthase (NADPH) activity
C	0006537	biological_process	glutamate biosynthetic process
C	0008652	biological_process	amino acid biosynthetic process
C	0015930	molecular_function	glutamate synthase activity
C	0016491	molecular_function	oxidoreductase activity
C	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
C	0019676	biological_process	ammonia assimilation cycle
C	0046872	molecular_function	metal ion binding
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051538	molecular_function	3 iron, 4 sulfur cluster binding
C	0097054	biological_process	L-glutamate biosynthetic process
D	0004355	molecular_function	glutamate synthase (NADPH) activity
D	0006537	biological_process	glutamate biosynthetic process
D	0008652	biological_process	amino acid biosynthetic process
D	0015930	molecular_function	glutamate synthase activity
D	0016491	molecular_function	oxidoreductase activity
D	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
D	0019676	biological_process	ammonia assimilation cycle
D	0046872	molecular_function	metal ion binding
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051538	molecular_function	3 iron, 4 sulfur cluster binding
D	0097054	biological_process	L-glutamate biosynthetic process
E	0004355	molecular_function	glutamate synthase (NADPH) activity
E	0006537	biological_process	glutamate biosynthetic process
E	0008652	biological_process	amino acid biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0046872	molecular_function	metal ion binding
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051539	molecular_function	4 iron, 4 sulfur cluster binding
E	0097054	biological_process	L-glutamate biosynthetic process
F	0004355	molecular_function	glutamate synthase (NADPH) activity
F	0006537	biological_process	glutamate biosynthetic process
F	0008652	biological_process	amino acid biosynthetic process
F	0016491	molecular_function	oxidoreductase activity
F	0046872	molecular_function	metal ion binding
F	0051536	molecular_function	iron-sulfur cluster binding
F	0051539	molecular_function	4 iron, 4 sulfur cluster binding
F	0097054	biological_process	L-glutamate biosynthetic process
G	0004355	molecular_function	glutamate synthase (NADPH) activity
G	0006537	biological_process	glutamate biosynthetic process
G	0008652	biological_process	amino acid biosynthetic process
G	0016491	molecular_function	oxidoreductase activity
G	0046872	molecular_function	metal ion binding
G	0051536	molecular_function	iron-sulfur cluster binding
G	0051539	molecular_function	4 iron, 4 sulfur cluster binding
G	0097054	biological_process	L-glutamate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue FMN A 1501

Chain	Residue
A	PRO856
A	GLY1028
A	GLY1029
A	ASP1070
A	GLY1071
A	GLY1072
A	ILE1092
A	GLY1093
A	THR1094
A	GLY857
A	SER859
A	GLU886
A	GLN909
A	LYS931
A	GLN934
A	LYS999
A	SER1027

site_id	AC2
Number of Residues	9
Details	binding site for residue F3S A 1502

Chain	Residue
A	MET479
A	CYS1102
A	ILE1103
A	MET1104
A	VAL1105
A	ARG1106
A	CYS1108
A	CYS1113
A	CYS1118

site_id	AC3
Number of Residues	18
Details	binding site for residue FMN B 1501

Chain	Residue
B	PRO856
B	GLY857
B	MET858
B	SER859
B	GLN909
B	LYS931
B	GLN934
B	LYS999
B	SER1027
B	GLY1028
B	GLY1029
B	THR1030
B	ASP1070
B	GLY1071
B	GLY1072
B	ILE1092
B	GLY1093
B	THR1094

site_id	AC4
Number of Residues	8
Details	binding site for residue F3S B 1502

Chain	Residue
B	CYS1102
B	MET1104
B	VAL1105
B	ARG1106
B	GLN1107
B	CYS1108
B	CYS1113
B	PRO1114

site_id	AC5
Number of Residues	18
Details	binding site for residue FMN C 1501

Chain	Residue
C	MET479
C	PRO856
C	GLY857
C	MET858
C	SER859
C	GLN909
C	LYS931
C	GLN934
C	LYS999
C	SER1027
C	GLY1028
C	GLY1029
C	THR1030
C	GLY1071
C	GLY1072
C	ILE1092
C	GLY1093
C	THR1094

site_id	AC6
Number of Residues	10
Details	binding site for residue F3S C 1502

Chain	Residue
C	MET479
C	CYS1102
C	MET1104
C	VAL1105
C	ARG1106
C	GLN1107
C	CYS1108
C	CYS1113
C	VAL1115
C	CYS1118

site_id	AC7
Number of Residues	14
Details	binding site for residue FMN D 1501

Chain	Residue
D	PRO856
D	SER859
D	GLU886
D	LYS931
D	LYS999
D	SER1027
D	GLY1028
D	GLY1029
D	ASP1070
D	GLY1071
D	GLY1072
D	ILE1092
D	GLY1093
D	THR1094

site_id	AC8
Number of Residues	17
Details	binding site for residue FAD E 503

Chain	Residue
E	TYR177
E	ASP178
E	ARG179
E	GLY185
E	LEU186
E	VAL221
E	THR241
E	GLY242
E	TYR244
E	ASP300
E	ASP443
E	SER449
E	ILE98
E	GLY155
E	GLY157
E	PRO158
E	ALA159

site_id	AC9
Number of Residues	7
Details	binding site for residue SF4 F 501

Chain	Residue
F	CYS48
F	SER49
F	CYS51
F	CYS56
F	CYS109
F	VAL110
F	VAL119

site_id	AD1
Number of Residues	7
Details	binding site for residue SF4 F 502

Chain	Residue
F	CYS60
F	CYS95
F	CYS99
F	CYS105
F	GLY122
F	GLU125
F	VAL452

site_id	AD2
Number of Residues	17
Details	binding site for residue FAD F 503

Chain	Residue
F	ILE98
F	GLY155
F	GLY157
F	PRO158
F	ALA159
F	ASP178
F	ARG179
F	GLY185
F	LEU186
F	VAL221
F	ALA240
F	THR241
F	TYR244
F	ASP304
F	ASP443
F	SER449
F	LEU450

site_id	AD3
Number of Residues	8
Details	binding site for residue SF4 G 502

Chain	Residue
G	CYS60
G	ASN64
G	CYS95
G	CYS99
G	CYS105
G	ILE121
G	GLY122
G	GLU125

site_id	AD4
Number of Residues	21
Details	binding site for residue FAD G 503

Chain	Residue
G	ILE98
G	GLY155
G	ALA156
G	GLY157
G	PRO158
G	ASP178
G	ARG179
G	GLY185
G	LEU186
G	GLY190
G	ILE191
G	PHE219
G	VAL221
G	ALA240
G	THR241
G	GLY242
G	TYR244
G	ASP304
G	ASP443
G	SER449
G	VAL451

site_id	AD5
Number of Residues	12
Details	binding site for Di-peptide F3S D 1502 and CYS D 1113

Chain	Residue
D	CYS1102
D	ILE1103
D	MET1104
D	VAL1105
D	ARG1106
D	CYS1108
D	THR1112
D	PRO1114
D	VAL1115
D	GLY1116
D	VAL1119
D	LEU1124

site_id	AD6
Number of Residues	9
Details	binding site for Di-peptide SF4 E 501 and CYS E 56

Chain	Residue
E	CYS48
E	CYS51
E	PRO54
E	PHE55
E	GLN57
E	VAL58
E	ILE66
E	CYS109
E	VAL110

site_id	AD7
Number of Residues	10
Details	binding site for Di-peptide SF4 E 501 and CYS E 109

Chain	Residue
E	CYS48
E	CYS51
E	CYS56
E	ILE66
E	GLU106
E	ASN108
E	VAL110
E	ILE111
E	GLU112
E	GLN113

site_id	AD8
Number of Residues	10
Details	binding site for Di-peptide SF4 E 502 and CYS E 105

Chain	Residue
E	CYS60
E	VAL62
E	ASN64
E	CYS95
E	CYS99
E	GLN101
E	LEU104
E	GLU106
E	GLY107
E	GLU125

site_id	AD9
Number of Residues	10
Details	binding site for Di-peptide SF4 G 501 and CYS G 51

Chain	Residue
D	VAL1105
G	CYS48
G	SER49
G	GLN50
G	GLY52
G	VAL53
G	PRO54
G	CYS56
G	CYS109
G	VAL110

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1580
Details	Domain: {"description":"Glutamine amidotransferase type-2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00609","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	84
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	40
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Active site: {"description":"For GATase activity","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	464
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	99
Details	Domain: {"description":"4Fe-4S ferredoxin-type"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	12
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 304

Chain	Residue	Details
A	CYS1	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
A	ASN231	electrostatic stabiliser, hydrogen bond donor
A	GLY232	electrostatic stabiliser, hydrogen bond donor
A	MET479	single electron acceptor, single electron donor, single electron relay
A	GLU886	proton acceptor, proton donor, proton relay
A	LYS937	electrostatic stabiliser

site_id	MCSA2
Number of Residues	6
Details	M-CSA 304

Chain	Residue	Details
B	CYS1	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
B	ASN231	electrostatic stabiliser, hydrogen bond donor
B	GLY232	electrostatic stabiliser, hydrogen bond donor
B	MET479	single electron acceptor, single electron donor, single electron relay
B	GLU886	proton acceptor, proton donor, proton relay
B	LYS937	electrostatic stabiliser

site_id	MCSA3
Number of Residues	6
Details	M-CSA 304

Chain	Residue	Details
C	CYS1	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
C	ASN231	electrostatic stabiliser, hydrogen bond donor
C	GLY232	electrostatic stabiliser, hydrogen bond donor
C	MET479	single electron acceptor, single electron donor, single electron relay
C	GLU886	proton acceptor, proton donor, proton relay
C	LYS937	electrostatic stabiliser

site_id	MCSA4
Number of Residues	6
Details	M-CSA 304

Chain	Residue	Details
D	CYS1	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
D	ASN231	electrostatic stabiliser, hydrogen bond donor
D	GLY232	electrostatic stabiliser, hydrogen bond donor
D	MET479	single electron acceptor, single electron donor, single electron relay
D	GLU886	proton acceptor, proton donor, proton relay
D	LYS937	electrostatic stabiliser

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