Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4JE5

Crystal structure of the aromatic aminotransferase Aro8, a putative alpha-aminoadipate aminotransferase in Saccharomyces cerevisiae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0006571	biological_process	tyrosine biosynthetic process
A	0008483	molecular_function	transaminase activity
A	0008793	molecular_function	aromatic-amino-acid transaminase activity
A	0009058	biological_process	biosynthetic process
A	0009072	biological_process	aromatic amino acid metabolic process
A	0009074	biological_process	aromatic amino acid family catabolic process
A	0009094	biological_process	L-phenylalanine biosynthetic process
A	0019509	biological_process	L-methionine salvage from methylthioadenosine
A	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
A	0030170	molecular_function	pyridoxal phosphate binding
A	0047536	molecular_function	2-aminoadipate transaminase activity
A	0080130	molecular_function	L-phenylalanine-2-oxoglutarate transaminase activity
B	0005737	cellular_component	cytoplasm
B	0006571	biological_process	tyrosine biosynthetic process
B	0008483	molecular_function	transaminase activity
B	0008793	molecular_function	aromatic-amino-acid transaminase activity
B	0009058	biological_process	biosynthetic process
B	0009072	biological_process	aromatic amino acid metabolic process
B	0009074	biological_process	aromatic amino acid family catabolic process
B	0009094	biological_process	L-phenylalanine biosynthetic process
B	0019509	biological_process	L-methionine salvage from methylthioadenosine
B	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
B	0030170	molecular_function	pyridoxal phosphate binding
B	0047536	molecular_function	2-aminoadipate transaminase activity
B	0080130	molecular_function	L-phenylalanine-2-oxoglutarate transaminase activity
C	0005737	cellular_component	cytoplasm
C	0006571	biological_process	tyrosine biosynthetic process
C	0008483	molecular_function	transaminase activity
C	0008793	molecular_function	aromatic-amino-acid transaminase activity
C	0009058	biological_process	biosynthetic process
C	0009072	biological_process	aromatic amino acid metabolic process
C	0009074	biological_process	aromatic amino acid family catabolic process
C	0009094	biological_process	L-phenylalanine biosynthetic process
C	0019509	biological_process	L-methionine salvage from methylthioadenosine
C	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
C	0030170	molecular_function	pyridoxal phosphate binding
C	0047536	molecular_function	2-aminoadipate transaminase activity
C	0080130	molecular_function	L-phenylalanine-2-oxoglutarate transaminase activity
D	0005737	cellular_component	cytoplasm
D	0006571	biological_process	tyrosine biosynthetic process
D	0008483	molecular_function	transaminase activity
D	0008793	molecular_function	aromatic-amino-acid transaminase activity
D	0009058	biological_process	biosynthetic process
D	0009072	biological_process	aromatic amino acid metabolic process
D	0009074	biological_process	aromatic amino acid family catabolic process
D	0009094	biological_process	L-phenylalanine biosynthetic process
D	0019509	biological_process	L-methionine salvage from methylthioadenosine
D	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
D	0030170	molecular_function	pyridoxal phosphate binding
D	0047536	molecular_function	2-aminoadipate transaminase activity
D	0080130	molecular_function	L-phenylalanine-2-oxoglutarate transaminase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP A 601

Chain	Residue
A	GLY140
A	SER302
A	SER304
A	LYS305
A	ARG312
A	HOH740
B	TYR105
A	ASN141
A	THR142
A	PHE166
A	ILE215
A	ASN220
A	ASP248
A	PRO250
A	TYR251

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE EPE A 602

Chain	Residue
A	PRO63
A	LYS274
A	ASP276
A	HIS277
A	HOH788
D	TYR80
D	THR81
D	ASN83
D	ALA91
D	SER94
D	ARG351

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EPE A 603

Chain	Residue
A	GLU174
A	SER442
A	TRP443
A	LYS445
A	GLU447
A	HOH840
A	HOH940
D	LYS21

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE EPE B 604

Chain	Residue
A	LEU25
A	LYS26
A	GLY42
A	GLY43
A	TYR105
B	PHE166
B	ASN220
B	LYS305
B	PHE399
B	ARG470
B	PMP1000
B	HOH1214

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PMP B 1000

Chain	Residue
A	TYR105
B	GLY140
B	ASN141
B	THR142
B	PHE166
B	ILE215
B	ASN220
B	ASP248
B	PRO250
B	TYR251
B	SER302
B	SER304
B	LYS305
B	ARG312
B	EPE604
B	HOH1139
B	HOH1214

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PMP C 1000

Chain	Residue
C	GLY140
C	ASN141
C	THR142
C	PHE166
C	ILE215
C	ASN220
C	ASP248
C	TYR251
C	SER302
C	SER304
C	LYS305
C	ARG312
C	EPE1001
D	TYR105

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EPE C 1001

Chain	Residue
C	PHE166
C	ASN220
C	ARG470
C	PMP1000
D	GLY42
D	GLY43
D	TYR105
D	SER108

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EPE C 1002

Chain	Residue
C	GLU174
C	SER442
C	TRP443
C	LYS445
C	HOH1238
C	HOH1295

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18407956

Chain	Residue	Details
D	SER100
B	SER100
C	SER100

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