5WML

Arabidopsis thaliana Prephenate Aminotransferase mutant- K306A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
A	0005829	cellular_component	cytosol
A	0008483	molecular_function	transaminase activity
A	0008652	biological_process	amino acid biosynthetic process
A	0009058	biological_process	biosynthetic process
A	0009094	biological_process	L-phenylalanine biosynthetic process
A	0009095	biological_process	aromatic amino acid family biosynthetic process, prephenate pathway
A	0009507	cellular_component	chloroplast
A	0009536	cellular_component	plastid
A	0009570	cellular_component	chloroplast stroma
A	0009793	biological_process	embryo development ending in seed dormancy
A	0016740	molecular_function	transferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0033853	molecular_function	aspartate-prephenate aminotransferase activity
A	0033854	molecular_function	glutamate-prephenate aminotransferase activity
B	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
B	0005829	cellular_component	cytosol
B	0008483	molecular_function	transaminase activity
B	0008652	biological_process	amino acid biosynthetic process
B	0009058	biological_process	biosynthetic process
B	0009094	biological_process	L-phenylalanine biosynthetic process
B	0009095	biological_process	aromatic amino acid family biosynthetic process, prephenate pathway
B	0009507	cellular_component	chloroplast
B	0009536	cellular_component	plastid
B	0009570	cellular_component	chloroplast stroma
B	0009793	biological_process	embryo development ending in seed dormancy
B	0016740	molecular_function	transferase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0033853	molecular_function	aspartate-prephenate aminotransferase activity
B	0033854	molecular_function	glutamate-prephenate aminotransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue PMP A 501

Chain	Residue
A	GLY167
A	SER305
A	ARG314
A	GLU502
A	HOH659
B	TYR132
A	ALA168
A	LYS169
A	LEU172
A	TRP193
A	CYS239
A	ASN243
A	ASP272
A	TYR275

---

site_id	AC2
Number of Residues	12
Details	binding site for residue GLU A 502

Chain	Residue
A	THR84
A	MET85
A	ALA105
A	ALA106
A	GLY107
A	LYS169
A	TRP193
A	ASN243
A	TYR395
A	ARG445
A	PMP501
A	HOH608

---

site_id	AC3
Number of Residues	16
Details	binding site for residue PMP B 501

Chain	Residue
A	TYR132
B	GLY167
B	ALA168
B	LYS169
B	TRP193
B	CYS239
B	ASN243
B	ASP272
B	ILE274
B	TYR275
B	SER305
B	ARG314
B	TYR395
B	GLU502
B	HOH637
B	HOH676

---

site_id	AC4
Number of Residues	12
Details	binding site for residue GLU B 502

Chain	Residue
B	SER82
B	THR84
B	MET85
B	ALA106
B	GLY107
B	LYS169
B	TRP193
B	VAL194
B	ASN243
B	TYR395
B	ARG445
B	PMP501

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	GLY107
A	TRP193
A	ASN243
A	ARG445
B	GLY107
B	TRP193
B	ASN243
B	ARG445

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250

Chain	Residue	Details
A	ALA306
B	ALA306

---