Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4ATP

Structure of GABA-transaminase A1R958 from Arthrobacter aurescens in complex with PLP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003867	molecular_function	4-aminobutyrate transaminase activity
A	0008483	molecular_function	transaminase activity
A	0009448	biological_process	gamma-aminobutyric acid metabolic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
A	0042802	molecular_function	identical protein binding
B	0003867	molecular_function	4-aminobutyrate transaminase activity
B	0008483	molecular_function	transaminase activity
B	0009448	biological_process	gamma-aminobutyric acid metabolic process
B	0030170	molecular_function	pyridoxal phosphate binding
B	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
B	0042802	molecular_function	identical protein binding
C	0003867	molecular_function	4-aminobutyrate transaminase activity
C	0008483	molecular_function	transaminase activity
C	0009448	biological_process	gamma-aminobutyric acid metabolic process
C	0030170	molecular_function	pyridoxal phosphate binding
C	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
C	0042802	molecular_function	identical protein binding
D	0003867	molecular_function	4-aminobutyrate transaminase activity
D	0008483	molecular_function	transaminase activity
D	0009448	biological_process	gamma-aminobutyric acid metabolic process
D	0030170	molecular_function	pyridoxal phosphate binding
D	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
D	0042802	molecular_function	identical protein binding
E	0003867	molecular_function	4-aminobutyrate transaminase activity
E	0008483	molecular_function	transaminase activity
E	0009448	biological_process	gamma-aminobutyric acid metabolic process
E	0030170	molecular_function	pyridoxal phosphate binding
E	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
E	0042802	molecular_function	identical protein binding
F	0003867	molecular_function	4-aminobutyrate transaminase activity
F	0008483	molecular_function	transaminase activity
F	0009448	biological_process	gamma-aminobutyric acid metabolic process
F	0030170	molecular_function	pyridoxal phosphate binding
F	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
F	0042802	molecular_function	identical protein binding
G	0003867	molecular_function	4-aminobutyrate transaminase activity
G	0008483	molecular_function	transaminase activity
G	0009448	biological_process	gamma-aminobutyric acid metabolic process
G	0030170	molecular_function	pyridoxal phosphate binding
G	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
G	0042802	molecular_function	identical protein binding
H	0003867	molecular_function	4-aminobutyrate transaminase activity
H	0008483	molecular_function	transaminase activity
H	0009448	biological_process	gamma-aminobutyric acid metabolic process
H	0030170	molecular_function	pyridoxal phosphate binding
H	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
H	0042802	molecular_function	identical protein binding
I	0003867	molecular_function	4-aminobutyrate transaminase activity
I	0008483	molecular_function	transaminase activity
I	0009448	biological_process	gamma-aminobutyric acid metabolic process
I	0030170	molecular_function	pyridoxal phosphate binding
I	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
I	0042802	molecular_function	identical protein binding
J	0003867	molecular_function	4-aminobutyrate transaminase activity
J	0008483	molecular_function	transaminase activity
J	0009448	biological_process	gamma-aminobutyric acid metabolic process
J	0030170	molecular_function	pyridoxal phosphate binding
J	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
J	0042802	molecular_function	identical protein binding
K	0003867	molecular_function	4-aminobutyrate transaminase activity
K	0008483	molecular_function	transaminase activity
K	0009448	biological_process	gamma-aminobutyric acid metabolic process
K	0030170	molecular_function	pyridoxal phosphate binding
K	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
K	0042802	molecular_function	identical protein binding
L	0003867	molecular_function	4-aminobutyrate transaminase activity
L	0008483	molecular_function	transaminase activity
L	0009448	biological_process	gamma-aminobutyric acid metabolic process
L	0030170	molecular_function	pyridoxal phosphate binding
L	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
L	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP A 500

Chain	Residue
A	SER133
A	LYS295
A	HOH2086
A	HOH2100
A	HOH2120
B	THR324
A	GLY134
A	ALA135
A	TYR161
A	HIS162
A	GLU233
A	ASP266
A	VAL268
A	GLN269

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

Chain	Residue
A	THR324
A	HOH2048
B	SER133
B	GLY134
B	ALA135
B	TYR161
B	HIS162
B	GLU233
B	ASP266
B	VAL268
B	GLN269
B	LYS295
B	HOH2039
B	HOH2076

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP C 500

Chain	Residue
C	SER133
C	GLY134
C	ALA135
C	TYR161
C	HIS162
C	GLU233
C	ASP266
C	VAL268
C	GLN269
C	LYS295
C	HOH2048
C	HOH2078
C	HOH2095
D	THR324

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

Chain	Residue
C	THR324
D	SER133
D	GLY134
D	ALA135
D	TYR161
D	HIS162
D	GLU233
D	ASP266
D	VAL268
D	GLN269
D	LYS295
D	HOH2028
D	HOH2030
D	HOH2031
D	HOH2056

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

Chain	Residue
E	SER133
E	GLY134
E	ALA135
E	TYR161
E	HIS162
E	GLU233
E	ASP266
E	VAL268
E	GLN269
E	LYS295
E	HOH2085
E	HOH2095
E	HOH2109
E	HOH2110
F	THR324

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP F 500

Chain	Residue
E	THR324
E	HOH2056
E	HOH2098
F	SER133
F	GLY134
F	ALA135
F	TYR161
F	HIS162
F	GLU233
F	ASP266
F	VAL268
F	GLN269
F	LYS295
F	HOH2044
F	HOH2062

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PLP G 500

Chain	Residue
G	SER133
G	GLY134
G	ALA135
G	TYR161
G	HIS162
G	GLU233
G	ASP266
G	GLN269
G	LYS295
G	HOH2032
H	THR324

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PLP H 500

Chain	Residue
H	SER133
H	GLY134
H	ALA135
H	TYR161
H	HIS162
H	GLU233
H	ASP266
H	VAL268
H	GLN269
H	LYS295
G	THR324

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PLP I 500

Chain	Residue
I	SER133
I	GLY134
I	ALA135
I	TYR161
I	GLU233
I	ASP266
I	VAL268
I	GLN269
I	LYS295
I	HOH2012
L	THR324

site_id	BC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP J 500

Chain	Residue
J	SER133
J	GLY134
J	ALA135
J	TYR161
J	HIS162
J	GLU233
J	ASP266
J	VAL268
J	GLN269
J	LYS295
J	HOH2018
J	HOH2022
K	THR324

site_id	BC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP K 500

Chain	Residue
J	THR324
J	HOH2007
K	SER133
K	GLY134
K	ALA135
K	TYR161
K	HIS162
K	GLU233
K	ASP266
K	GLN269
K	LYS295
K	HOH2009

site_id	BC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP L 500

Chain	Residue
I	THR324
L	SER133
L	GLY134
L	ALA135
L	TYR161
L	HIS162
L	GLU233
L	ASP266
L	VAL268
L	GLN269
L	LYS295
L	HOH2011

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FIaDEVqs.GFcRtGewfavdhegvvp....DIItmAKgiaGG

Chain	Residue	Details
A	PHE263-GLY300

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