Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2ZY3

dodecameric L-aspartate beta-decarboxylase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
A	0006523	biological_process	alanine biosynthetic process
A	0006531	biological_process	aspartate metabolic process
A	0008483	molecular_function	transaminase activity
A	0008652	biological_process	amino acid biosynthetic process
A	0009058	biological_process	biosynthetic process
A	0016831	molecular_function	carboxy-lyase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042802	molecular_function	identical protein binding
A	0047688	molecular_function	aspartate 4-decarboxylase activity
B	0003824	molecular_function	catalytic activity
B	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
B	0006523	biological_process	alanine biosynthetic process
B	0006531	biological_process	aspartate metabolic process
B	0008483	molecular_function	transaminase activity
B	0008652	biological_process	amino acid biosynthetic process
B	0009058	biological_process	biosynthetic process
B	0016831	molecular_function	carboxy-lyase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042802	molecular_function	identical protein binding
B	0047688	molecular_function	aspartate 4-decarboxylase activity
C	0003824	molecular_function	catalytic activity
C	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
C	0006523	biological_process	alanine biosynthetic process
C	0006531	biological_process	aspartate metabolic process
C	0008483	molecular_function	transaminase activity
C	0008652	biological_process	amino acid biosynthetic process
C	0009058	biological_process	biosynthetic process
C	0016831	molecular_function	carboxy-lyase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0042802	molecular_function	identical protein binding
C	0047688	molecular_function	aspartate 4-decarboxylase activity
D	0003824	molecular_function	catalytic activity
D	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
D	0006523	biological_process	alanine biosynthetic process
D	0006531	biological_process	aspartate metabolic process
D	0008483	molecular_function	transaminase activity
D	0008652	biological_process	amino acid biosynthetic process
D	0009058	biological_process	biosynthetic process
D	0016831	molecular_function	carboxy-lyase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0042802	molecular_function	identical protein binding
D	0047688	molecular_function	aspartate 4-decarboxylase activity
E	0003824	molecular_function	catalytic activity
E	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
E	0006523	biological_process	alanine biosynthetic process
E	0006531	biological_process	aspartate metabolic process
E	0008483	molecular_function	transaminase activity
E	0008652	biological_process	amino acid biosynthetic process
E	0009058	biological_process	biosynthetic process
E	0016831	molecular_function	carboxy-lyase activity
E	0030170	molecular_function	pyridoxal phosphate binding
E	0042802	molecular_function	identical protein binding
E	0047688	molecular_function	aspartate 4-decarboxylase activity
F	0003824	molecular_function	catalytic activity
F	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
F	0006523	biological_process	alanine biosynthetic process
F	0006531	biological_process	aspartate metabolic process
F	0008483	molecular_function	transaminase activity
F	0008652	biological_process	amino acid biosynthetic process
F	0009058	biological_process	biosynthetic process
F	0016831	molecular_function	carboxy-lyase activity
F	0030170	molecular_function	pyridoxal phosphate binding
F	0042802	molecular_function	identical protein binding
F	0047688	molecular_function	aspartate 4-decarboxylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP A 900

Chain	Residue
A	ARG37
A	TYR289
A	SER312
A	SER314
A	LYS315
A	ARG323
B	TYR134
A	GLY173
A	GLY174
A	THR175
A	PHE204
A	VAL252
A	ASN256
A	ASP286
A	VAL288

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP B 900

Chain	Residue
A	TYR134
B	ARG37
B	GLY173
B	GLY174
B	THR175
B	PHE204
B	VAL252
B	ASN256
B	ASP286
B	TYR289
B	SER312
B	SER314
B	LYS315
B	ARG323

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP C 900

Chain	Residue
C	ARG37
C	GLY173
C	GLY174
C	THR175
C	PHE204
C	ASN256
C	ASP286
C	VAL288
C	TYR289
C	SER312
C	SER314
C	LYS315
C	ARG323
D	TYR134

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP D 900

Chain	Residue
C	TYR134
D	ARG37
D	GLY173
D	GLY174
D	THR175
D	PHE204
D	VAL252
D	ASN256
D	ASP286
D	VAL288
D	TYR289
D	SER312
D	SER314
D	LYS315
D	ARG323

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP E 900

Chain	Residue
E	ARG37
E	TYR134
E	GLY173
E	GLY174
E	THR175
E	PHE204
E	ASN256
E	ASP286
E	TYR289
E	SER312
E	SER314
E	LYS315
E	ARG323

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP F 900

Chain	Residue
F	ARG37
F	TYR134
F	GLY173
F	GLY174
F	THR175
F	PHE204
F	ASN256
F	ASP286
F	TYR289
F	SER312
F	SER314
F	LYS315
F	ARG323

Functional Information from PROSITE/UniProt

site_id	PS00105
Number of Residues	14
Details	AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKyfGAtGWRLG

Chain	Residue	Details
A	SER312-GLY325

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	GLY115
D	GLY115
D	ASN256
D	ARG497
E	GLY115
E	ASN256
E	ARG497
F	GLY115
F	ASN256
F	ARG497
A	ASN256
A	ARG497
B	GLY115
B	ASN256
B	ARG497
C	GLY115
C	ASN256
C	ARG497

site_id	SWS_FT_FI2
Number of Residues	6
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269\|PubMed:19368885, ECO:0007744\|PDB:2ZY3, ECO:0007744\|PDB:2ZY4, ECO:0007744\|PDB:2ZY5

Chain	Residue	Details
A	LYS315
B	LYS315
C	LYS315
D	LYS315
E	LYS315
F	LYS315

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	PHE204
A	ASP286
A	LYS315

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
B	PHE204
B	ASP286
B	LYS315

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
C	PHE204
C	ASP286
C	LYS315

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
D	PHE204
D	ASP286
D	LYS315

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
E	PHE204
E	ASP286
E	LYS315

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
F	PHE204
F	ASP286
F	LYS315

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