Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1PMO

Crystal structure of Escherichia coli GadB (neutral pH)

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	L-glutamate catabolic process
A	0016020	cellular_component	membrane
A	0016829	molecular_function	lyase activity
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	L-glutamate catabolic process
B	0016020	cellular_component	membrane
B	0016829	molecular_function	lyase activity
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	L-glutamate catabolic process
C	0016020	cellular_component	membrane
C	0016829	molecular_function	lyase activity
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	L-glutamate catabolic process
D	0016020	cellular_component	membrane
D	0016829	molecular_function	lyase activity
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	L-glutamate catabolic process
E	0016020	cellular_component	membrane
E	0016829	molecular_function	lyase activity
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	L-glutamate catabolic process
F	0016020	cellular_component	membrane
F	0016829	molecular_function	lyase activity
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	16
Details	BINDING SITE FOR RESIDUE PLR A 1500

Chain	Residue
A	GLY125
A	HIS465
A	THR466
A	HOH3266
A	HOH3314
A	HOH3427
B	PHE317
B	SER318
A	SER126
A	SER127
A	GLN163
A	THR212
A	ASP243
A	ALA245
A	HIS275
A	LYS276

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLR B 1501

Chain	Residue
A	PHE317
A	SER318
A	HOH3307
B	GLY125
B	SER126
B	SER127
B	GLN163
B	THR212
B	ASP243
B	ALA245
B	SER273
B	HIS275
B	LYS276
B	HIS465
B	HOH3316
B	HOH3425

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PLR 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	THR466
C	HOH3317
C	HOH3326
D	PHE317
D	SER318
D	HOH3310

site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLR D 1503

Chain	Residue
C	PHE317
C	SER318
C	HOH3364
D	GLY125
D	SER126
D	SER127
D	GLN163
D	THR212
D	ASP243
D	ALA245
D	SER273
D	HIS275
D	LYS276
D	HIS465
D	THR466
D	HOH3328
D	HOH3422

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLR E 1504

Chain	Residue
E	SER126
E	SER127
E	GLN163
E	THR212
E	ASP243
E	ALA245
E	SER273
E	HIS275
E	LYS276
E	HIS465
E	THR466
E	HOH3315
E	HOH3319
F	PHE317
F	SER318
F	HOH3295

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLR F 1505

Chain	Residue
F	HOH3318
E	PHE317
E	SER318
F	GLY125
F	SER126
F	SER127
F	GLN163
F	THR212
F	ASP243
F	ALA245
F	SER273
F	HIS275
F	LYS276
F	HIS465
F	THR466
F	HOH3267
F	HOH3313

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TRS A 3236

Chain	Residue
A	GLN65
A	THR66
A	TRP67
A	ASP69
A	VAL72
A	LEU279
A	ALA280
A	PRO281
A	GLU330
A	ARG427
A	HOH3255
A	HOH3305
A	HOH3437
B	ILE80
B	ASN81

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS B 3237

Chain	Residue
A	ILE80
A	ASN81
B	GLN65
B	TRP67
B	VAL72
B	LEU279
B	ALA280
B	PRO281
B	GLU330
B	ARG427

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRS D 3238

Chain	Residue
C	ASN81
D	GLN65
D	TRP67
D	ASP69
D	VAL72
D	LEU279
D	GLU330
D	ARG427
D	HOH3363

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TRS E 3239

Chain	Residue
E	GLN65
E	THR66
E	TRP67
E	ASP69
E	VAL72
E	LEU279
E	ALA280
E	ARG427
E	HOH3380
E	HOH3437
F	ASN81

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS F 3240

Chain	Residue
E	ASN81
F	GLN65
F	TRP67
F	VAL72
F	LEU279
F	ALA280
F	PRO281
F	GLU330
F	ARG427
F	HOH3286

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRS A 3241

Chain	Residue
A	VAL119
A	GLY120
A	THR121
A	VAL300
A	GLY311
A	PHE313
A	TRS3251
A	HOH3372
A	HOH3438

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TRS B 3242

Chain	Residue
B	TRP84
B	LYS87
B	ASP97
B	LEU98
B	GLY120
B	THR121
B	ASN122
B	HOH3390

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TRS C 3243

Chain	Residue
C	TRP84
C	LYS87
C	ASP97
C	GLY120
C	THR121
C	ASN122
C	THR312
C	HOH3442

site_id	BC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS D 3244

Chain	Residue
D	TRP84
D	ASP97
D	LEU98
D	VAL101
D	GLY120
D	THR121
D	ASN122
D	THR312
D	TRS3245
D	HOH3359

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS D 3245

Chain	Residue
D	VAL119
D	GLY120
D	THR121
D	GLY311
D	THR312
D	PHE313
D	TRS3244

site_id	BC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS E 3246

Chain	Residue
E	TRP84
E	LYS87
E	ASP97
E	LEU98
E	VAL101
E	GLY120
E	THR121
E	ASN122
E	THR312
E	TRS3247

site_id	BC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS E 3247

Chain	Residue
E	VAL119
E	GLY120
E	LEU295
E	VAL300
E	GLY311
E	THR312
E	PHE313
E	TRS3246
E	HOH3342
E	HOH3410

site_id	CC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS F 3248

Chain	Residue
F	TRP84
F	ASP97
F	LEU98
F	VAL101
F	GLY120
F	THR121
F	ASN122
F	GLY311
F	THR312
F	TRS3249

site_id	CC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS F 3249

Chain	Residue
F	VAL119
F	GLY120
F	THR121
F	LEU295
F	GLY311
F	THR312
F	PHE313
F	TRS3248
F	HOH3423
F	HOH3438

site_id	CC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS C 3250

Chain	Residue
C	GLN65
C	TRP67
C	ASP69
C	VAL72
C	LEU279
C	ALA280
C	PRO281
C	GLU330
C	HOH3399
D	ASN81

site_id	CC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS A 3251

Chain	Residue
A	TRP84
A	ASP97
A	LEU98
A	VAL101
A	GLY120
A	THR121
A	ASN122
A	TRS3241
A	HOH3288
A	HOH3439

site_id	CC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TRS C 3252

Chain	Residue
A	PRO91
A	GLN92
B	LEU52
C	GLN58
C	ARG402
C	LEU436
C	ASP440
C	HOH3407

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE TRS E 3253

Chain	Residue
E	PRO184
E	GLY185
E	LEU187
E	GLU364
E	LYS381
E	ILE418

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 site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	18
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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