Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2DGK

Crystal structure of an N-terminal deletion mutant of Escherichia coli GadB in an autoinhibited state (aldamine)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004351	molecular_function	glutamate decarboxylase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006536	biological_process	glutamate metabolic process
A	0006538	biological_process	glutamate catabolic process
A	0016020	cellular_component	membrane
A	0016830	molecular_function	carbon-carbon lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	0051454	biological_process	intracellular pH elevation
B	0004351	molecular_function	glutamate decarboxylase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006536	biological_process	glutamate metabolic process
B	0006538	biological_process	glutamate catabolic process
B	0016020	cellular_component	membrane
B	0016830	molecular_function	carbon-carbon lyase activity
B	0016831	molecular_function	carboxy-lyase activity
B	0019752	biological_process	carboxylic acid metabolic process
B	0030170	molecular_function	pyridoxal phosphate binding
B	0051454	biological_process	intracellular pH elevation
C	0004351	molecular_function	glutamate decarboxylase activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006536	biological_process	glutamate metabolic process
C	0006538	biological_process	glutamate catabolic process
C	0016020	cellular_component	membrane
C	0016830	molecular_function	carbon-carbon lyase activity
C	0016831	molecular_function	carboxy-lyase activity
C	0019752	biological_process	carboxylic acid metabolic process
C	0030170	molecular_function	pyridoxal phosphate binding
C	0051454	biological_process	intracellular pH elevation
D	0004351	molecular_function	glutamate decarboxylase activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006536	biological_process	glutamate metabolic process
D	0006538	biological_process	glutamate catabolic process
D	0016020	cellular_component	membrane
D	0016830	molecular_function	carbon-carbon lyase activity
D	0016831	molecular_function	carboxy-lyase activity
D	0019752	biological_process	carboxylic acid metabolic process
D	0030170	molecular_function	pyridoxal phosphate binding
D	0051454	biological_process	intracellular pH elevation
E	0004351	molecular_function	glutamate decarboxylase activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006536	biological_process	glutamate metabolic process
E	0006538	biological_process	glutamate catabolic process
E	0016020	cellular_component	membrane
E	0016830	molecular_function	carbon-carbon lyase activity
E	0016831	molecular_function	carboxy-lyase activity
E	0019752	biological_process	carboxylic acid metabolic process
E	0030170	molecular_function	pyridoxal phosphate binding
E	0051454	biological_process	intracellular pH elevation
F	0004351	molecular_function	glutamate decarboxylase activity
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006536	biological_process	glutamate metabolic process
F	0006538	biological_process	glutamate catabolic process
F	0016020	cellular_component	membrane
F	0016830	molecular_function	carbon-carbon lyase activity
F	0016831	molecular_function	carboxy-lyase activity
F	0019752	biological_process	carboxylic acid metabolic process
F	0030170	molecular_function	pyridoxal phosphate binding
F	0051454	biological_process	intracellular pH elevation

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 4770

Chain	Residue
A	PRO113
A	LYS114
A	ASP291
A	GLU292
A	HOH5007
A	HOH5008

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 4771

Chain	Residue
B	HOH4952
B	HOH4994
B	HOH5041
B	LYS114
B	ASP291
B	GLU292

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 4772

Chain	Residue
C	LYS114
C	ASP291
C	GLU292
C	HOH4881
C	HOH4889
C	HOH4993

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 4773

Chain	Residue
D	PRO113
D	LYS114
D	ASP291
D	GLU292
D	HOH5003
D	HOH5044
D	HOH5045

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 E 4774

Chain	Residue
E	LYS114
E	ASP291
E	GLU292

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 F 4775

Chain	Residue
F	LYS114
F	ASP291
F	GLU292
F	HOH4963

site_id	AC7
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP A 1500

Chain	Residue
A	GLY125
A	SER126
A	SER127
A	GLN163
A	CYS165
A	THR208
A	THR212
A	ASP243
A	ALA245
A	SER273
A	HIS275
A	LYS276
A	HIS465
A	HOH4774
A	HOH4783
B	PHE317
B	SER318

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP B 1501

Chain	Residue
A	PHE317
A	SER318
B	GLY125
B	SER126
B	SER127
B	GLN163
B	THR208
B	THR212
B	ASP243
B	ALA245
B	SER273
B	HIS275
B	LYS276
B	HIS465
B	HOH4782
B	HOH4888

site_id	AC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP C 1502

Chain	Residue
C	GLY125
C	SER126
C	SER127
C	GLN163
C	THR208
C	THR212
C	ASP243
C	ALA245
C	SER273
C	HIS275
C	LYS276
C	HIS465
C	HOH4830
D	PHE317
D	SER318
D	HOH4779

site_id	BC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP D 1503

Chain	Residue
C	PHE317
C	SER318
D	GLY125
D	SER126
D	SER127
D	GLN163
D	CYS165
D	THR208
D	THR212
D	ASP243
D	ALA245
D	SER273
D	HIS275
D	LYS276
D	HIS465
D	HOH4777
D	HOH4825

site_id	BC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP E 1504

Chain	Residue
E	SER126
E	SER127
E	GLN163
E	CYS165
E	THR208
E	THR212
E	ASP243
E	ALA245
E	SER273
E	HIS275
E	LYS276
E	HIS465
E	HOH4794
E	HOH4824
F	PHE317
F	SER318
E	GLY125

site_id	BC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PLP F 1505

Chain	Residue
E	PHE317
E	SER318
E	HOH4790
F	GLY125
F	SER126
F	SER127
F	GLN163
F	CYS165
F	THR208
F	GLY210
F	THR212
F	ASP243
F	ALA245
F	SER273
F	HIS275
F	LYS276
F	HIS465
F	HOH4898

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 2191

Chain	Residue
A	ASN81
A	HOH4779
B	ARG57
B	ASP68
C	TYR51

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 2192

Chain	Residue
B	TYR51
C	ARG57
C	ASP68
C	HOH4982
D	ASN81

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 2193

Chain	Residue
A	GLN92
A	ARG99
A	HOH4970
B	GLU49
C	ASP432

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 2194

Chain	Residue
A	GLU49
B	GLN92
B	ARG99
B	HOH4808
F	ASP432

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 2195

Chain	Residue
C	GLN92
C	ARG99
C	HOH4988
D	GLU49
D	LEU52
E	ASP432

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO D 2196

Chain	Residue
B	ASP432
B	LEU436
C	GLU49
D	GLN92
D	ARG99
D	HOH4938

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO E 2197

Chain	Residue
A	ASP432
E	GLN92
E	ARG99
E	HOH4879
F	GLU49
F	LEU52

site_id	CC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO F 2198

Chain	Residue
D	ASP432
D	PHE433
D	LEU436
E	GLU49
E	LEU52
F	GLN92
F	ARG99
F	HOH4942

Functional Information from PROSITE/UniProt

site_id	PS00392
Number of Residues	22
Details	DDC_GAD_HDC_YDC DDC / GAD / HDC / TyrDC pyridoxal-phosphate attachment site. SIsAsghKFGlApLGCgwVIwR

Chain	Residue	Details
A	SER269-ARG290

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	BINDING:

Chain	Residue	Details
A	THR62
B	HIS275
C	THR62
C	ASN83
C	SER126
C	THR212
C	HIS275
D	THR62
D	ASN83
D	SER126
D	THR212
A	ASN83
D	HIS275
E	THR62
E	ASN83
E	SER126
E	THR212
E	HIS275
F	THR62
F	ASN83
F	SER126
F	THR212
A	SER126
F	HIS275
A	THR212
A	HIS275
B	THR62
B	ASN83
B	SER126
B	THR212

site_id	SWS_FT_FI2
Number of Residues	6
Details	MOD_RES: N6-(pyridoxal phosphate)lysine

Chain	Residue	Details
A	LYS276
B	LYS276
C	LYS276
D	LYS276
E	LYS276
F	LYS276

site_id	SWS_FT_FI3
Number of Residues	18
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:18723842

Chain	Residue	Details
A	LYS446
D	LYS446
D	LYS453
D	LYS464
E	LYS446
E	LYS453
E	LYS464
F	LYS446
F	LYS453
F	LYS464
A	LYS453
A	LYS464
B	LYS446
B	LYS453
B	LYS464
C	LYS446
C	LYS453
C	LYS464

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