Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5YB0

Crystal Structure of Wild Type Phosphoserine aminotransferase (PSAT) from E. histolytica

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
A	0005737	cellular_component	cytoplasm
A	0006563	biological_process	L-serine metabolic process
A	0006564	biological_process	L-serine biosynthetic process
A	0008483	molecular_function	transaminase activity
A	0008652	biological_process	amino acid biosynthetic process
A	0016740	molecular_function	transferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
B	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
B	0005737	cellular_component	cytoplasm
B	0006563	biological_process	L-serine metabolic process
B	0006564	biological_process	L-serine biosynthetic process
B	0008483	molecular_function	transaminase activity
B	0008652	biological_process	amino acid biosynthetic process
B	0016740	molecular_function	transferase activity
B	0030170	molecular_function	pyridoxal phosphate binding
C	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
C	0005737	cellular_component	cytoplasm
C	0006563	biological_process	L-serine metabolic process
C	0006564	biological_process	L-serine biosynthetic process
C	0008483	molecular_function	transaminase activity
C	0008652	biological_process	amino acid biosynthetic process
C	0016740	molecular_function	transferase activity
C	0030170	molecular_function	pyridoxal phosphate binding
D	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
D	0005737	cellular_component	cytoplasm
D	0006563	biological_process	L-serine metabolic process
D	0006564	biological_process	L-serine biosynthetic process
D	0008483	molecular_function	transaminase activity
D	0008652	biological_process	amino acid biosynthetic process
D	0016740	molecular_function	transferase activity
D	0030170	molecular_function	pyridoxal phosphate binding
E	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
E	0005737	cellular_component	cytoplasm
E	0006563	biological_process	L-serine metabolic process
E	0006564	biological_process	L-serine biosynthetic process
E	0008483	molecular_function	transaminase activity
E	0008652	biological_process	amino acid biosynthetic process
E	0016740	molecular_function	transferase activity
E	0030170	molecular_function	pyridoxal phosphate binding
F	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
F	0005737	cellular_component	cytoplasm
F	0006563	biological_process	L-serine metabolic process
F	0006564	biological_process	L-serine biosynthetic process
F	0008483	molecular_function	transaminase activity
F	0008652	biological_process	amino acid biosynthetic process
F	0016740	molecular_function	transferase activity
F	0030170	molecular_function	pyridoxal phosphate binding
G	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
G	0005737	cellular_component	cytoplasm
G	0006563	biological_process	L-serine metabolic process
G	0006564	biological_process	L-serine biosynthetic process
G	0008483	molecular_function	transaminase activity
G	0008652	biological_process	amino acid biosynthetic process
G	0016740	molecular_function	transferase activity
G	0030170	molecular_function	pyridoxal phosphate binding
H	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
H	0005737	cellular_component	cytoplasm
H	0006563	biological_process	L-serine metabolic process
H	0006564	biological_process	L-serine biosynthetic process
H	0008483	molecular_function	transaminase activity
H	0008652	biological_process	amino acid biosynthetic process
H	0016740	molecular_function	transferase activity
H	0030170	molecular_function	pyridoxal phosphate binding
I	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
I	0005737	cellular_component	cytoplasm
I	0006563	biological_process	L-serine metabolic process
I	0006564	biological_process	L-serine biosynthetic process
I	0008483	molecular_function	transaminase activity
I	0008652	biological_process	amino acid biosynthetic process
I	0016740	molecular_function	transferase activity
I	0030170	molecular_function	pyridoxal phosphate binding
J	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
J	0005737	cellular_component	cytoplasm
J	0006563	biological_process	L-serine metabolic process
J	0006564	biological_process	L-serine biosynthetic process
J	0008483	molecular_function	transaminase activity
J	0008652	biological_process	amino acid biosynthetic process
J	0016740	molecular_function	transferase activity
J	0030170	molecular_function	pyridoxal phosphate binding
K	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
K	0005737	cellular_component	cytoplasm
K	0006563	biological_process	L-serine metabolic process
K	0006564	biological_process	L-serine biosynthetic process
K	0008483	molecular_function	transaminase activity
K	0008652	biological_process	amino acid biosynthetic process
K	0016740	molecular_function	transferase activity
K	0030170	molecular_function	pyridoxal phosphate binding
L	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
L	0005737	cellular_component	cytoplasm
L	0006563	biological_process	L-serine metabolic process
L	0006564	biological_process	L-serine biosynthetic process
L	0008483	molecular_function	transaminase activity
L	0008652	biological_process	amino acid biosynthetic process
L	0016740	molecular_function	transferase activity
L	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue PLP A 401

Chain	Residue
A	GLY76
A	LYS191
B	ASN232
B	THR233
A	ALA77
A	SER78
A	TRP101
A	ASN146
A	THR148
A	ASP167
A	SER169
A	GLN190

site_id	AC2
Number of Residues	3
Details	binding site for residue CL A 402

Chain	Residue
A	GLY99
A	VAL100
A	TRP101

site_id	AC3
Number of Residues	2
Details	binding site for residue CL B 402

Chain	Residue
B	VAL100
B	TRP101

site_id	AC4
Number of Residues	4
Details	binding site for residue CL C 402

Chain	Residue
C	VAL100
C	ASN147
C	THR148
C	ILE149

site_id	AC5
Number of Residues	3
Details	binding site for residue CL D 402

Chain	Residue
D	VAL100
D	TRP101
D	ILE149

site_id	AC6
Number of Residues	5
Details	binding site for residue CL E 402

Chain	Residue
E	VAL100
E	TRP101
E	ASN147
E	THR148
E	ILE149

site_id	AC7
Number of Residues	12
Details	binding site for residue PLP H 401

Chain	Residue
E	ASN232
E	THR233
H	GLY76
H	ALA77
H	SER78
H	PHE81
H	TRP101
H	THR144
H	THR148
H	SER169
H	GLN190
H	LYS191

site_id	AC8
Number of Residues	9
Details	binding site for residue PLP K 401

Chain	Residue
K	GLY76
K	ALA77
K	SER78
K	TRP101
K	ASN146
K	THR148
K	ASP167
K	SER169
L	THR233

site_id	AC9
Number of Residues	13
Details	binding site for Di-peptide PLP B 401 and LYS B 191

Chain	Residue
A	ASN232
A	THR233
B	GLY76
B	ALA77
B	SER78
B	TRP101
B	THR148
B	ASP167
B	SER169
B	ALA189
B	GLN190
B	ASN192
B	TYR334

site_id	AD1
Number of Residues	14
Details	binding site for Di-peptide PLP C 401 and LYS C 191

Chain	Residue
C	ALA11
C	GLY76
C	ALA77
C	SER78
C	TRP101
C	THR144
C	THR148
C	ASP167
C	SER169
C	ALA189
C	GLN190
C	ASN192
D	ASN232
D	THR233

site_id	AD2
Number of Residues	15
Details	binding site for Di-peptide PLP D 401 and LYS D 191

Chain	Residue
C	ASN232
C	THR233
D	GLY76
D	ALA77
D	SER78
D	PHE81
D	TRP101
D	THR144
D	THR148
D	ASP167
D	SER169
D	ALA189
D	GLN190
D	ASN192
D	TYR334

site_id	AD3
Number of Residues	13
Details	binding site for Di-peptide PLP E 401 and LYS E 191

Chain	Residue
E	SER169
E	ALA189
E	GLN190
E	ASN192
E	TYR334
H	THR233
E	GLY76
E	ALA77
E	SER78
E	PHE81
E	TRP101
E	THR144
E	ASP167

site_id	AD4
Number of Residues	13
Details	binding site for Di-peptide PLP F 401 and LYS F 191

Chain	Residue
F	GLY76
F	ALA77
F	SER78
F	PHE81
F	TRP101
F	THR148
F	ASP167
F	SER169
F	ALA189
F	GLN190
F	ASN192
G	ASN232
G	THR233

site_id	AD5
Number of Residues	17
Details	binding site for Di-peptide PLP G 401 and LYS G 191

Chain	Residue
F	ASN232
F	THR233
G	GLY76
G	ALA77
G	SER78
G	PHE81
G	TRP101
G	THR144
G	THR148
G	ASP167
G	SER169
G	SER170
G	ALA189
G	GLN190
G	ASN192
G	TYR334
G	HOH506

site_id	AD6
Number of Residues	15
Details	binding site for Di-peptide PLP I 401 and LYS I 191

Chain	Residue
I	GLY76
I	ALA77
I	SER78
I	PHE81
I	TRP101
I	THR144
I	THR148
I	ASP167
I	SER169
I	ALA189
I	GLN190
I	ASN192
I	TYR334
J	ASN232
J	THR233

site_id	AD7
Number of Residues	15
Details	binding site for Di-peptide PLP I 401 and LYS I 191

Chain	Residue
I	GLY76
I	ALA77
I	SER78
I	PHE81
I	TRP101
I	THR144
I	THR148
I	ASP167
I	SER169
I	ALA189
I	GLN190
I	ASN192
I	TYR334
J	ASN232
J	THR233

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