Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1PMM

Crystal structure of Escherichia coli GadB (low 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 PLP A 500

Chain	Residue
A	GLY125
A	SER273
A	HIS275
A	LYS276
A	HOH5552
A	HOH5567
B	PHE317
B	SER318
A	SER126
A	SER127
A	GLN163
A	CYS165
A	THR208
A	THR212
A	ASP243
A	ALA245

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP B 500

Chain	Residue
A	PHE317
A	SER318
B	GLY125
B	SER126
B	SER127
B	GLN163
B	CYS165
B	THR208
B	THR212
B	ASP243
B	ALA245
B	SER273
B	HIS275
B	LYS276
B	HOH6552
B	HOH6574

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP C 501

Chain	Residue
C	GLY125
C	SER126
C	SER127
C	GLN163
C	CYS165
C	THR208
C	THR212
C	ASP243
C	ALA245
C	SER273
C	HIS275
C	LYS276
C	HOH8528
D	PHE317
D	SER318
D	HOH7561

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP D 501

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	HOH7538
D	HOH7566

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP E 502

Chain	Residue
E	GLY125
E	SER126
E	SER127
E	GLN163
E	CYS165
E	THR208
E	THR212
E	ASP243
E	ALA245
E	SER273
E	HIS275
E	LYS276
E	HOH9548
F	PHE317
F	SER318
F	HOH520

site_id	AC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP F 502

Chain	Residue
E	PHE317
E	SER318
E	HOH9562
F	GLY125
F	SER126
F	SER127
F	GLN163
F	CYS165
F	THR208
F	THR212
F	ASP243
F	ALA245
F	SER273
F	HIS275
F	LYS276
F	HOH544

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACY A 5518

Chain	Residue
A	SER318
A	HOH5654
B	THR62
B	PHE63
A	ASN83
A	ASP86
A	PHE317

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACY B 6518

Chain	Residue
A	THR62
A	PHE63
B	ASN83
B	ASP86
B	SER318
B	HOH6689

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY D 7518

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

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACY C 8518

Chain	Residue
C	THR62
C	PHE63
C	HOH8740
D	ASN83
D	ASP86
D	SER318

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACY E 9518

Chain	Residue
E	ASN83
E	ASP86
E	SER318
E	HOH9537
F	THR62
F	PHE63

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACY E 9519

Chain	Residue
E	THR62
E	PHE63
E	HOH9678
F	ASN83
F	ASP86
F	SER318

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	6
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)