Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3FSL

Crystal structure of tyrosine aminotransferase tripple mutant (P181Q,R183G,A321K) from Escherichia coli at 2.35 A resolution

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	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006520	biological_process	amino acid metabolic process
A	0006532	biological_process	aspartate biosynthetic process
A	0006571	biological_process	tyrosine biosynthetic process
A	0008483	molecular_function	transaminase activity
A	0008652	biological_process	amino acid biosynthetic process
A	0008793	molecular_function	aromatic-amino-acid transaminase activity
A	0009058	biological_process	biosynthetic process
A	0009073	biological_process	aromatic amino acid family biosynthetic process
A	0009094	biological_process	L-phenylalanine biosynthetic process
A	0009098	biological_process	L-leucine biosynthetic process
A	0019292	biological_process	L-tyrosine biosynthetic process from chorismate via 4-hydroxyphenylpyruvate
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	0042803	molecular_function	protein homodimerization activity
A	0080130	molecular_function	L-phenylalanine-2-oxoglutarate transaminase activity
B	0003824	molecular_function	catalytic activity
B	0004838	molecular_function	L-tyrosine-2-oxoglutarate transaminase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006520	biological_process	amino acid metabolic process
B	0006532	biological_process	aspartate biosynthetic process
B	0006571	biological_process	tyrosine biosynthetic process
B	0008483	molecular_function	transaminase activity
B	0008652	biological_process	amino acid biosynthetic process
B	0008793	molecular_function	aromatic-amino-acid transaminase activity
B	0009058	biological_process	biosynthetic process
B	0009073	biological_process	aromatic amino acid family biosynthetic process
B	0009094	biological_process	L-phenylalanine biosynthetic process
B	0009098	biological_process	L-leucine biosynthetic process
B	0019292	biological_process	L-tyrosine biosynthetic process from chorismate via 4-hydroxyphenylpyruvate
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	0042803	molecular_function	protein homodimerization activity
B	0080130	molecular_function	L-phenylalanine-2-oxoglutarate transaminase activity
C	0003824	molecular_function	catalytic activity
C	0004838	molecular_function	L-tyrosine-2-oxoglutarate transaminase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006520	biological_process	amino acid metabolic process
C	0006532	biological_process	aspartate biosynthetic process
C	0006571	biological_process	tyrosine biosynthetic process
C	0008483	molecular_function	transaminase activity
C	0008652	biological_process	amino acid biosynthetic process
C	0008793	molecular_function	aromatic-amino-acid transaminase activity
C	0009058	biological_process	biosynthetic process
C	0009073	biological_process	aromatic amino acid family biosynthetic process
C	0009094	biological_process	L-phenylalanine biosynthetic process
C	0009098	biological_process	L-leucine biosynthetic process
C	0019292	biological_process	L-tyrosine biosynthetic process from chorismate via 4-hydroxyphenylpyruvate
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	0042803	molecular_function	protein homodimerization activity
C	0080130	molecular_function	L-phenylalanine-2-oxoglutarate transaminase activity
D	0003824	molecular_function	catalytic activity
D	0004838	molecular_function	L-tyrosine-2-oxoglutarate transaminase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006520	biological_process	amino acid metabolic process
D	0006532	biological_process	aspartate biosynthetic process
D	0006571	biological_process	tyrosine biosynthetic process
D	0008483	molecular_function	transaminase activity
D	0008652	biological_process	amino acid biosynthetic process
D	0008793	molecular_function	aromatic-amino-acid transaminase activity
D	0009058	biological_process	biosynthetic process
D	0009073	biological_process	aromatic amino acid family biosynthetic process
D	0009094	biological_process	L-phenylalanine biosynthetic process
D	0009098	biological_process	L-leucine biosynthetic process
D	0019292	biological_process	L-tyrosine biosynthetic process from chorismate via 4-hydroxyphenylpyruvate
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	0042803	molecular_function	protein homodimerization activity
D	0080130	molecular_function	L-phenylalanine-2-oxoglutarate transaminase activity
E	0003824	molecular_function	catalytic activity
E	0004838	molecular_function	L-tyrosine-2-oxoglutarate transaminase activity
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006520	biological_process	amino acid metabolic process
E	0006532	biological_process	aspartate biosynthetic process
E	0006571	biological_process	tyrosine biosynthetic process
E	0008483	molecular_function	transaminase activity
E	0008652	biological_process	amino acid biosynthetic process
E	0008793	molecular_function	aromatic-amino-acid transaminase activity
E	0009058	biological_process	biosynthetic process
E	0009073	biological_process	aromatic amino acid family biosynthetic process
E	0009094	biological_process	L-phenylalanine biosynthetic process
E	0009098	biological_process	L-leucine biosynthetic process
E	0019292	biological_process	L-tyrosine biosynthetic process from chorismate via 4-hydroxyphenylpyruvate
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	0042803	molecular_function	protein homodimerization activity
E	0080130	molecular_function	L-phenylalanine-2-oxoglutarate transaminase activity
F	0003824	molecular_function	catalytic activity
F	0004838	molecular_function	L-tyrosine-2-oxoglutarate transaminase activity
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006520	biological_process	amino acid metabolic process
F	0006532	biological_process	aspartate biosynthetic process
F	0006571	biological_process	tyrosine biosynthetic process
F	0008483	molecular_function	transaminase activity
F	0008652	biological_process	amino acid biosynthetic process
F	0008793	molecular_function	aromatic-amino-acid transaminase activity
F	0009058	biological_process	biosynthetic process
F	0009073	biological_process	aromatic amino acid family biosynthetic process
F	0009094	biological_process	L-phenylalanine biosynthetic process
F	0009098	biological_process	L-leucine biosynthetic process
F	0019292	biological_process	L-tyrosine biosynthetic process from chorismate via 4-hydroxyphenylpyruvate
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	0042803	molecular_function	protein homodimerization activity
F	0080130	molecular_function	L-phenylalanine-2-oxoglutarate transaminase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLR A 500

Chain	Residue
A	GLY107
A	SER257
A	LYS258
A	ARG266
B	TYR70
A	GLY108
A	SER109
A	TRP140
A	ASN194
A	ASP222
A	ALA224
A	TYR225
A	SER255

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

Chain	Residue
A	TYR70
A	HOH1063
B	GLY107
B	GLY108
B	SER109
B	TRP140
B	ASN194
B	ASP222
B	ALA224
B	TYR225
B	SER255
B	SER257
B	LYS258
B	ARG266

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

Chain	Residue
A	HOH1170
C	GLY107
C	GLY108
C	SER109
C	TRP140
C	ASN194
C	ASP222
C	ALA224
C	TYR225
C	SER255
C	SER257
C	LYS258
C	ARG266
D	TYR70

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLR D 500

Chain	Residue
A	HOH419
C	TYR70
D	GLY107
D	GLY108
D	SER109
D	TRP140
D	ASN194
D	ASP222
D	ALA224
D	TYR225
D	SER255
D	SER257
D	LYS258
D	ARG266

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLR E 500

Chain	Residue
E	GLY107
E	GLY108
E	SER109
E	TRP140
E	ASN194
E	ASP222
E	ALA224
E	TYR225
E	SER255
E	SER257
E	LYS258
E	ARG266
F	TYR70

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLR F 500

Chain	Residue
A	HOH563
E	TYR70
F	GLY107
F	GLY108
F	SER109
F	TRP140
F	ASN194
F	ASP222
F	ALA224
F	TYR225
F	SER255
F	SER257
F	LYS258
F	ARG266

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER255-GLY268

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	GLY38
B	ASN194
B	ARG292
B	ARG386
C	GLY38
C	TYR70
C	TRP140
C	ASN194
C	ARG292
C	ARG386
D	GLY38
A	TYR70
D	TYR70
D	TRP140
D	ASN194
D	ARG292
D	ARG386
E	GLY38
E	TYR70
E	TRP140
E	ASN194
E	ARG292
A	TRP140
E	ARG386
F	GLY38
F	TYR70
F	TRP140
F	ASN194
F	ARG292
F	ARG386
A	ASN194
A	ARG292
A	ARG386
B	GLY38
B	TYR70
B	TRP140

site_id	SWS_FT_FI2
Number of Residues	6
Details	MOD_RES: N6-(pyridoxal phosphate)lysine

Chain	Residue	Details
A	LYS258
B	LYS258
C	LYS258
D	LYS258
E	LYS258
F	LYS258

Catalytic Information from CSA

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

Chain	Residue	Details
A	TRP140
A	ASP222
A	LYS258

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

Chain	Residue	Details
B	TRP140
B	ASP222
B	LYS258

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

Chain	Residue	Details
C	TRP140
C	ASP222
C	LYS258

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

Chain	Residue	Details
D	TRP140
D	ASP222
D	LYS258

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

Chain	Residue	Details
E	TRP140
E	ASP222
E	LYS258

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

Chain	Residue	Details
F	TRP140
F	ASP222
F	LYS258

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
D	TRP140
D	ASP222

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
E	TRP140
E	ASP222

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
F	TRP140
F	ASP222

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