Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2DGM

Crystal structure of Escherichia coli GadB in complex with iodide

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	2
Details	BINDING SITE FOR RESIDUE IOD A 2331

Chain	Residue
A	SER16
F	ARG427

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD B 2332

Chain	Residue
B	SER16
C	ARG427

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD B 2333

Chain	Residue
B	ARG427
C	SER16

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD D 2334

Chain	Residue
D	SER16
E	ARG427

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD E 2335

Chain	Residue
E	SER16
D	ARG427

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD F 2336

Chain	Residue
A	ARG427
F	SER16

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD A 2337

Chain	Residue
A	LYS381
A	ILE418

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD B 2338

Chain	Residue
B	ILE418

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD C 2339

Chain	Residue
C	LYS381
C	ILE418

site_id	BC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD F 2342

Chain	Residue
F	ILE418

site_id	BC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD A 2343

Chain	Residue
A	LYS453

site_id	BC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD D 2346

Chain	Residue
D	LYS453

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD E 2347

Chain	Residue
E	HIS451

site_id	BC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD F 2348

Chain	Residue
F	LYS453

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD A 2349

Chain	Residue
A	TRP67
A	HIS73

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IOD B 2350

Chain	Residue
A	ASN81
B	ASP68
B	HIS73

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IOD C 2351

Chain	Residue
C	TRP67
C	ASP68
C	HIS73
D	ASN81

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IOD D 2352

Chain	Residue
C	ASN81
D	ASP68
D	HIS73

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IOD E 2353

Chain	Residue
E	TRP67
E	ASP68
E	HIS73
F	ASN81

site_id	CC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD F 2354

Chain	Residue
F	HIS73

site_id	CC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IOD A 2355

Chain	Residue
A	LEU382
A	THR391
A	LEU392

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IOD B 2356

Chain	Residue
B	LEU382
B	THR391
B	LEU392

site_id	CC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IOD C 2357

Chain	Residue
C	LEU382
C	THR391
C	LEU392

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IOD D 2358

Chain	Residue
D	LEU382
D	THR391
D	LEU392

site_id	CC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD E 2359

Chain	Residue
E	THR391
E	LEU392

site_id	CC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD F 2360

Chain	Residue
F	THR391
F	LEU392

site_id	CC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP A 500

Chain	Residue
A	GLY125
A	SER126
A	SER127
A	GLN163
A	THR208
A	THR212
A	ASP243
A	ALA245
A	SER273
A	HIS275
A	LYS276
A	HOH2651
B	PHE317
B	SER318
B	HOH2680

site_id	DC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP B 500

Chain	Residue
A	PHE317
A	SER318
A	HOH2637
B	GLY125
B	SER126
B	SER127
B	GLN163
B	CYS165
B	THR212
B	ASP243
B	ALA245
B	SER273
B	HIS275
B	LYS276
B	HOH2703

site_id	DC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP C 501

Chain	Residue
D	HOH2673
C	GLY125
C	SER126
C	SER127
C	GLN163
C	THR208
C	THR212
C	ASP243
C	ALA245
C	SER273
C	HIS275
C	LYS276
C	HOH2619
D	PHE317
D	SER318

site_id	DC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP D 501

Chain	Residue
C	PHE317
C	SER318
C	HOH2649
D	GLY125
D	SER126
D	SER127
D	GLN163
D	CYS165
D	THR212
D	ASP243
D	ALA245
D	SER273
D	HIS275
D	LYS276
D	HOH2649

site_id	DC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP E 502

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	HOH2857
F	PHE317
F	SER318
F	HOH2688

site_id	DC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP F 502

Chain	Residue
E	PHE317
E	SER318
E	HOH2869
F	GLY125
F	SER126
F	SER127
F	GLN163
F	CYS165
F	THR212
F	ASP243
F	ALA245
F	SER273
F	HIS275
F	LYS276
F	HOH2711

site_id	DC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 2550

Chain	Residue
A	ASN83
A	ASP86
B	THR62
B	PHE63

site_id	DC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 2560

Chain	Residue
A	THR62
A	PHE63
B	ASN83
B	ASP86

site_id	DC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT D 2570

Chain	Residue
C	ASN83
C	ASP86
D	THR62
D	PHE63

site_id	DC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT D 2580

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

site_id	EC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT F 2590

Chain	Residue
E	ASN83
E	ASP86
F	THR62
F	PHE63

site_id	EC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 2600

Chain	Residue
A	TRP84
A	ASP97
A	THR121
A	ASN122
A	HOH2720

site_id	EC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT C 2610

Chain	Residue
C	ASP97
C	LEU98
C	THR121
C	ASN122
C	HOH2725

site_id	EC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT E 2620

Chain	Residue
E	TRP84
E	ASP97
E	THR121
E	ASN122
E	HOH2973

site_id	EC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT D 2630

Chain	Residue
D	TRP84
D	ASP97
D	LEU98
D	GLY120
D	THR121
D	ASN122
D	HOH2778

site_id	EC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT F 2640

Chain	Residue
F	TRP84
F	ASP97
F	THR121
F	ASN122
F	HOH2726

site_id	EC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT B 2650

Chain	Residue
B	TRP84
B	ASP97
B	THR121
B	ASN122
B	HOH2707
B	HOH2848

site_id	EC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT F 2660

Chain	Residue
F	LEU98
F	ALA118
F	GLY120
F	GLY311

site_id	EC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT F 2670

Chain	Residue
F	PRO111
F	ARG290
F	ASP291
F	HOH2678
F	HOH2793
F	HOH2810

site_id	FC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACY E 2519

Chain	Residue
E	THR62
E	PHE63
F	ASN83
F	ASP86
F	PHE317
F	SER318

site_id	FC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PEG E 2833

Chain	Residue
E	ASP228
E	ASP237
E	ASP239
E	PRO265
E	ARG266
E	LYS268
E	HOH2933
E	HOH3104

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	11
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)