3FZ8

Crystal structure of glutamate decarboxylase beta from Escherichia coli: reduced Schiff base with PLP

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	15
Details	BINDING SITE FOR RESIDUE PLR A 500

Chain	Residue
A	SER126
A	HIS275
A	LYS276
A	HIS465
A	THR466
B	PHE317
B	SER318
A	SER127
A	GLN163
A	THR208
A	GLY210
A	THR212
A	ASP243
A	ALA245
A	SER273

---

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLR B 500

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	THR466

---

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLR C 500

Chain	Residue
C	SER126
C	SER127
C	GLN163
C	THR208
C	GLY210
C	THR212
C	ASP243
C	ALA245
C	SER273
C	HIS275
C	LYS276
C	HIS465
C	THR466
D	PHE317
D	SER318

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLR D 500

Chain	Residue
C	PHE317
C	SER318
D	GLY125
D	SER126
D	SER127
D	GLN163
D	THR208
D	THR212
D	ASP243
D	ALA245
D	SER273
D	HIS275
D	LYS276
D	HIS465
D	THR466

---

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLR E 500

Chain	Residue
E	GLY125
E	SER126
E	SER127
E	GLN163
E	THR208
E	GLY210
E	THR212
E	ASP243
E	ALA245
E	SER273
E	HIS275
E	LYS276
E	THR466
F	PHE317
F	SER318

---

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLR F 500

Chain	Residue
E	PHE317
E	SER318
F	GLY125
F	SER126
F	SER127
F	GLN163
F	GLY210
F	THR212
F	ASP243
F	ALA245
F	SER273
F	HIS275
F	LYS276
F	THR466

---

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

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