3FZ7

Crystal structure of apo glutamate decarboxylase beta from Escherichia coli

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	10
Details	BINDING SITE FOR RESIDUE PO4 A 467

Chain	Residue
A	GLY125
F	SER318
A	SER126
A	SER127
A	SER273
A	HIS275
A	LYS276
D	HOH1316
D	HOH1437
F	PHE317

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 F 467

Chain	Residue
A	PHE317
A	SER318
D	HOH813
D	HOH1058
D	HOH1193
D	HOH1288
F	SER126
F	SER127
F	SER273
F	HIS275
F	LYS276

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 D 467

Chain	Residue
D	GLY125
D	SER126
D	SER127
D	SER273
D	HIS275
D	LYS276
D	HOH1352
D	HOH1396
E	PHE317
E	SER318

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 B 467

Chain	Residue
B	SER126
B	SER127
B	SER273
B	HIS275
B	LYS276
C	PHE317
C	SER318
D	HOH1002
D	HOH1098

---

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 E 467

Chain	Residue
D	PHE317
D	SER318
D	HOH1256
E	GLY125
E	SER126
E	SER127
E	SER273
E	HIS275
E	LYS276

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 C 467

Chain	Residue
B	PHE317
B	SER318
C	GLY125
C	SER126
C	SER127
C	SER273
C	HIS275
C	LYS276
D	HOH1169

---

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

---