Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2VYC

Crystal Structure of Acid Induced Arginine Decarboxylase from E. coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006520	biological_process	amino acid metabolic process
A	0006527	biological_process	arginine catabolic process
A	0008792	molecular_function	arginine decarboxylase activity
A	0016829	molecular_function	lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0051454	biological_process	intracellular pH elevation
B	0003824	molecular_function	catalytic activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006520	biological_process	amino acid metabolic process
B	0006527	biological_process	arginine catabolic process
B	0008792	molecular_function	arginine decarboxylase activity
B	0016829	molecular_function	lyase activity
B	0016831	molecular_function	carboxy-lyase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0051454	biological_process	intracellular pH elevation
C	0003824	molecular_function	catalytic activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006520	biological_process	amino acid metabolic process
C	0006527	biological_process	arginine catabolic process
C	0008792	molecular_function	arginine decarboxylase activity
C	0016829	molecular_function	lyase activity
C	0016831	molecular_function	carboxy-lyase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0051454	biological_process	intracellular pH elevation
D	0003824	molecular_function	catalytic activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006520	biological_process	amino acid metabolic process
D	0006527	biological_process	arginine catabolic process
D	0008792	molecular_function	arginine decarboxylase activity
D	0016829	molecular_function	lyase activity
D	0016831	molecular_function	carboxy-lyase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0051454	biological_process	intracellular pH elevation
E	0003824	molecular_function	catalytic activity
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006520	biological_process	amino acid metabolic process
E	0006527	biological_process	arginine catabolic process
E	0008792	molecular_function	arginine decarboxylase activity
E	0016829	molecular_function	lyase activity
E	0016831	molecular_function	carboxy-lyase activity
E	0030170	molecular_function	pyridoxal phosphate binding
E	0051454	biological_process	intracellular pH elevation
F	0003824	molecular_function	catalytic activity
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006520	biological_process	amino acid metabolic process
F	0006527	biological_process	arginine catabolic process
F	0008792	molecular_function	arginine decarboxylase activity
F	0016829	molecular_function	lyase activity
F	0016831	molecular_function	carboxy-lyase activity
F	0030170	molecular_function	pyridoxal phosphate binding
F	0051454	biological_process	intracellular pH elevation
G	0003824	molecular_function	catalytic activity
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006520	biological_process	amino acid metabolic process
G	0006527	biological_process	arginine catabolic process
G	0008792	molecular_function	arginine decarboxylase activity
G	0016829	molecular_function	lyase activity
G	0016831	molecular_function	carboxy-lyase activity
G	0030170	molecular_function	pyridoxal phosphate binding
G	0051454	biological_process	intracellular pH elevation
H	0003824	molecular_function	catalytic activity
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0006520	biological_process	amino acid metabolic process
H	0006527	biological_process	arginine catabolic process
H	0008792	molecular_function	arginine decarboxylase activity
H	0016829	molecular_function	lyase activity
H	0016831	molecular_function	carboxy-lyase activity
H	0030170	molecular_function	pyridoxal phosphate binding
H	0051454	biological_process	intracellular pH elevation
I	0003824	molecular_function	catalytic activity
I	0005737	cellular_component	cytoplasm
I	0005829	cellular_component	cytosol
I	0006520	biological_process	amino acid metabolic process
I	0006527	biological_process	arginine catabolic process
I	0008792	molecular_function	arginine decarboxylase activity
I	0016829	molecular_function	lyase activity
I	0016831	molecular_function	carboxy-lyase activity
I	0030170	molecular_function	pyridoxal phosphate binding
I	0051454	biological_process	intracellular pH elevation
J	0003824	molecular_function	catalytic activity
J	0005737	cellular_component	cytoplasm
J	0005829	cellular_component	cytosol
J	0006520	biological_process	amino acid metabolic process
J	0006527	biological_process	arginine catabolic process
J	0008792	molecular_function	arginine decarboxylase activity
J	0016829	molecular_function	lyase activity
J	0016831	molecular_function	carboxy-lyase activity
J	0030170	molecular_function	pyridoxal phosphate binding
J	0051454	biological_process	intracellular pH elevation

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP A 1386

Chain	Residue
A	GLY229
A	SER383
A	HIS385
A	LYS386
C	THR420
C	THR421
C	SER422
A	THR230
A	SER231
A	ASN234
A	HIS255
A	SER257
A	ASP347
A	ALA349
A	TRP350

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP B 1386

Chain	Residue
B	GLY229
B	THR230
B	SER231
B	ASN234
B	HIS255
B	ASP347
B	ALA349
B	TRP350
B	SER383
B	HIS385
B	LYS386
B	THR420
B	THR421
B	SER422

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP C 1386

Chain	Residue
A	THR420
A	THR421
A	SER422
C	GLY229
C	THR230
C	SER231
C	ASN234
C	HIS255
C	ASP347
C	ALA349
C	TRP350
C	SER383
C	HIS385
C	LYS386

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP D 1386

Chain	Residue
D	GLY229
D	THR230
D	SER231
D	ASN234
D	HIS255
D	ASP347
D	ALA349
D	TRP350
D	SER383
D	HIS385
D	LYS386
E	THR420
E	THR421
E	SER422

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP E 1386

Chain	Residue
D	THR420
D	THR421
D	SER422
E	GLY229
E	THR230
E	SER231
E	HIS255
E	ASP347
E	ALA349
E	TRP350
E	SER383
E	HIS385
E	LYS386

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP F 1386

Chain	Residue
F	GLY229
F	THR230
F	SER231
F	ASN234
F	HIS255
F	ASP347
F	ALA349
F	TRP350
F	SER383
F	HIS385
F	LYS386
F	THR420
F	THR421
F	SER422

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP G 1386

Chain	Residue
G	GLY229
G	THR230
G	SER231
G	ASN234
G	HIS255
G	ASP347
G	ALA349
G	TRP350
G	SER383
G	HIS385
G	LYS386
J	THR420
J	THR421
J	SER422

site_id	AC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP H 1386

Chain	Residue
H	THR230
H	SER231
H	ASN234
H	HIS255
H	ASP347
H	ALA349
H	TRP350
H	SER383
H	HIS385
H	LYS386
I	THR420
I	THR421
I	SER422
H	GLY229

site_id	AC9
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP I 1386

Chain	Residue
H	THR420
H	THR421
H	SER422
I	GLY229
I	THR230
I	SER231
I	HIS255
I	ASP347
I	ALA349
I	TRP350
I	SER383
I	HIS385
I	LYS386

site_id	BC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP J 1386

Chain	Residue
G	THR420
G	THR421
G	SER422
J	GLY229
J	THR230
J	SER231
J	ASN234
J	HIS255
J	ASP347
J	ALA349
J	TRP350
J	SER383
J	HIS385
J	LYS386

Functional Information from PROSITE/UniProt

site_id	PS00703
Number of Residues	15
Details	OKR_DC_1 Orn/Lys/Arg decarboxylases family 1 pyridoxal-P attachment site. ThStHKllNAlSQAS

Chain	Residue	Details
A	THR381-SER395

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269\|PubMed:19298070, ECO:0007744\|PDB:2VYC

Chain	Residue	Details
A	LYS386
J	LYS386
B	LYS386
C	LYS386
D	LYS386
E	LYS386
F	LYS386
G	LYS386
H	LYS386
I	LYS386

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)