Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2DGL

Crystal structure of Escherichia coli GadB in complex with bromide

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	2
Details	BINDING SITE FOR RESIDUE BR A 467

Chain	Residue
A	SER16
F	ARG427

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BR F 467

Chain	Residue
E	ASN81
F	ASP68
F	HIS73

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE BR A 468

Chain	Residue
A	ARG17

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BR B 467

Chain	Residue
B	SER16
C	ARG427

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BR C 467

Chain	Residue
C	ASP68
C	HIS73
C	TRP67

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE BR B 468

Chain	Residue
B	ARG17

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BR B 469

Chain	Residue
B	ARG427
C	SER16

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BR B 470

Chain	Residue
A	ASN81
B	ASP68
B	HIS73

site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE BR C 468

Chain	Residue
C	ARG17

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BR D 467

Chain	Residue
D	SER16
E	ARG427

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BR E 467

Chain	Residue
E	ASP68
E	HIS73
F	ASN81

site_id	BC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE BR D 468

Chain	Residue
D	ARG17

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BR E 468

Chain	Residue
D	ARG427
E	SER16

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BR C 469

Chain	Residue
C	ASN81
D	ASP68
D	HIS73

site_id	BC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE BR E 469

Chain	Residue
E	ARG17

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BR F 468

Chain	Residue
A	ARG427
F	SER16

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BR A 469

Chain	Residue
A	ASP68
A	HIS73
B	ASN81

site_id	BC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE BR F 469

Chain	Residue
F	ARG17

site_id	CC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE BR A 470

Chain	Residue
A	ILE418

site_id	CC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BR B 471

Chain	Residue
B	LYS381
B	ILE418

site_id	CC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BR C 470

Chain	Residue
C	LYS381
C	ILE418

site_id	CC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE BR D 469

Chain	Residue
D	LYS381

site_id	CC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE BR E 470

Chain	Residue
E	ILE418

site_id	CC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP A 500

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

site_id	CC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP B 500

Chain	Residue
A	PHE317
A	SER318
B	GLY125
B	SER126
B	SER127
B	GLN163
B	THR212
B	ASP243
B	ALA245
B	SER273
B	HIS275
B	LYS276
B	HOH567

site_id	CC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP C 501

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

site_id	CC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP D 501

Chain	Residue
C	PHE317
C	SER318
D	SER126
D	SER127
D	GLN163
D	CYS165
D	THR212
D	ASP243
D	ALA245
D	SER273
D	HIS275
D	LYS276

site_id	DC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP E 502

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

site_id	DC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP F 502

Chain	Residue
E	PHE317
E	SER318
E	HOH529
F	GLY125
F	SER126
F	SER127
F	GLN163
F	THR208
F	THR212
F	ASP243
F	ALA245
F	SER273
F	HIS275
F	LYS276

site_id	DC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACY E 518

Chain	Residue
E	THR62
E	PHE63
F	ASP86

site_id	DC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY F 528

Chain	Residue
E	ASN83
E	ASP86
E	SER318
F	THR62
F	PHE63

site_id	DC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACY C 538

Chain	Residue
C	THR62
C	PHE63
D	ASP86
D	SER318

site_id	DC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACY C 548

Chain	Residue
C	ASN83
C	ASP86
C	PHE317
C	SER318
D	THR62
D	PHE63
D	CYS64

site_id	DC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY B 558

Chain	Residue
A	THR62
A	PHE63
A	CYS64
B	ASN83
B	ASP86

site_id	DC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY A 568

Chain	Residue
A	ASN83
A	ASP86
A	SER318
B	THR62
B	PHE63

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)