Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4RKD

Psychrophilic aromatic amino acids aminotransferase from Psychrobacter sp. B6 cocrystalized with aspartic acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004838	molecular_function	L-tyrosine-2-oxoglutarate transaminase activity
A	0005829	cellular_component	cytosol
A	0006520	biological_process	amino acid metabolic process
A	0008483	molecular_function	transaminase activity
A	0009058	biological_process	biosynthetic process
A	0016740	molecular_function	transferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0033585	biological_process	L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
B	0003824	molecular_function	catalytic activity
B	0004838	molecular_function	L-tyrosine-2-oxoglutarate transaminase activity
B	0005829	cellular_component	cytosol
B	0006520	biological_process	amino acid metabolic process
B	0008483	molecular_function	transaminase activity
B	0009058	biological_process	biosynthetic process
B	0016740	molecular_function	transferase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0033585	biological_process	L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
C	0003824	molecular_function	catalytic activity
C	0004838	molecular_function	L-tyrosine-2-oxoglutarate transaminase activity
C	0005829	cellular_component	cytosol
C	0006520	biological_process	amino acid metabolic process
C	0008483	molecular_function	transaminase activity
C	0009058	biological_process	biosynthetic process
C	0016740	molecular_function	transferase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0033585	biological_process	L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
D	0003824	molecular_function	catalytic activity
D	0004838	molecular_function	L-tyrosine-2-oxoglutarate transaminase activity
D	0005829	cellular_component	cytosol
D	0006520	biological_process	amino acid metabolic process
D	0008483	molecular_function	transaminase activity
D	0009058	biological_process	biosynthetic process
D	0016740	molecular_function	transferase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0033585	biological_process	L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
E	0003824	molecular_function	catalytic activity
E	0004838	molecular_function	L-tyrosine-2-oxoglutarate transaminase activity
E	0005829	cellular_component	cytosol
E	0006520	biological_process	amino acid metabolic process
E	0008483	molecular_function	transaminase activity
E	0009058	biological_process	biosynthetic process
E	0016740	molecular_function	transferase activity
E	0030170	molecular_function	pyridoxal phosphate binding
E	0033585	biological_process	L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
E	0042802	molecular_function	identical protein binding
E	0046872	molecular_function	metal ion binding
F	0003824	molecular_function	catalytic activity
F	0004838	molecular_function	L-tyrosine-2-oxoglutarate transaminase activity
F	0005829	cellular_component	cytosol
F	0006520	biological_process	amino acid metabolic process
F	0008483	molecular_function	transaminase activity
F	0009058	biological_process	biosynthetic process
F	0016740	molecular_function	transferase activity
F	0030170	molecular_function	pyridoxal phosphate binding
F	0033585	biological_process	L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
F	0042802	molecular_function	identical protein binding
F	0046872	molecular_function	metal ion binding
G	0003824	molecular_function	catalytic activity
G	0004838	molecular_function	L-tyrosine-2-oxoglutarate transaminase activity
G	0005829	cellular_component	cytosol
G	0006520	biological_process	amino acid metabolic process
G	0008483	molecular_function	transaminase activity
G	0009058	biological_process	biosynthetic process
G	0016740	molecular_function	transferase activity
G	0030170	molecular_function	pyridoxal phosphate binding
G	0033585	biological_process	L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
G	0042802	molecular_function	identical protein binding
G	0046872	molecular_function	metal ion binding
H	0003824	molecular_function	catalytic activity
H	0004838	molecular_function	L-tyrosine-2-oxoglutarate transaminase activity
H	0005829	cellular_component	cytosol
H	0006520	biological_process	amino acid metabolic process
H	0008483	molecular_function	transaminase activity
H	0009058	biological_process	biosynthetic process
H	0016740	molecular_function	transferase activity
H	0030170	molecular_function	pyridoxal phosphate binding
H	0033585	biological_process	L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
H	0042802	molecular_function	identical protein binding
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 401

Chain	Residue
A	HOH528
A	HOH530
A	HOH533
A	HOH594
B	HOH551
B	HOH552

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP A 402

Chain	Residue
A	TRP130
A	ASP211
A	ALA213
A	TYR214
A	SER243
A	SER245
A	LYS246
A	ARG254
B	TYR65
A	GLY102
A	GLY103
A	SER104

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE KET A 403

Chain	Residue
A	GLY34
A	GLY102
A	GLY103
A	SER104
A	TRP130
A	ASN183
A	ASP211
A	TYR214
A	SER243
A	SER245
A	LYS246
A	ARG254
B	TYR65
B	ARG280

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP B 401

Chain	Residue
A	TYR65
B	GLY102
B	GLY103
B	SER104
B	ASN183
B	ASP211
B	ALA213
B	TYR214
B	SER243
B	SER245
B	LYS246
B	ARG254

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 401

Chain	Residue
C	HOH523
C	HOH569
C	HOH575
D	HOH542
D	HOH569

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP C 402

Chain	Residue
C	GLY102
C	GLY103
C	SER104
C	TRP130
C	ASN183
C	ASP211
C	TYR214
C	SER243
C	SER245
C	LYS246
C	ARG254
C	HOH573
C	HOH574
D	TYR65

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE OAA C 403

Chain	Residue
C	TYR65
C	ARG280
C	HOH570
D	TRP130
D	PMP401

site_id	AC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PMP D 401

Chain	Residue
C	TYR65
C	OAA403
D	GLY102
D	GLY103
D	SER104
D	TRP130
D	ASN183
D	ASP211
D	ALA213
D	TYR214
D	SER243
D	SER245
D	LYS246
D	ARG254
D	HOH615

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG E 401

Chain	Residue
E	GLU112
E	HOH523
E	HOH524
F	GLU112
F	HOH543
F	HOH545
F	HOH567

site_id	BC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP E 402

Chain	Residue
E	LYS246
E	ARG254
F	TYR65
E	GLY102
E	GLY103
E	SER104
E	ASN183
E	ASP211
E	ALA213
E	TYR214
E	SER243
E	SER245

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE OAA E 403

Chain	Residue
E	GLU138
E	ASP141
E	ILE142
E	GLU143
E	HOH543
E	HOH544
E	HOH562

site_id	BC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE KET E 404

Chain	Residue
E	GLY34
E	GLY102
E	GLY103
E	SER104
E	TRP130
E	ASN183
E	ASP211
E	TYR214
E	SER243
E	SER245
E	LYS246
E	ARG254
E	HOH568
F	TYR65

site_id	BC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP F 401

Chain	Residue
E	TYR65
F	GLY102
F	GLY103
F	SER104
F	TRP130
F	HIS133
F	ASN183
F	ASP211
F	ALA213
F	TYR214
F	SER243
F	SER245
F	LYS246
F	ARG254

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG G 401

Chain	Residue
G	HOH543
G	HOH563
H	HOH543
H	HOH544
H	HOH570
H	HOH571

site_id	BC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE KET G 402

Chain	Residue
G	GLY102
G	GLY103
G	SER104
G	TRP130
G	ASN183
G	ASP211
G	TYR214
G	SER243
G	SER245
G	LYS246
G	ARG254
G	ARG374
H	TYR65

site_id	BC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PMP H 401

Chain	Residue
G	TYR65
H	GLY102
H	GLY103
H	SER104
H	TRP130
H	ASN183
H	ASP211
H	ALA213
H	TYR214
H	SER243
H	SER245
H	LYS246
H	ARG254
H	HOH574

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER243-GLY256

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