Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8A5V

Crystal structure of the human phosposerine aminotransferase (PSAT)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006563	biological_process	L-serine metabolic process
A	0006564	biological_process	L-serine biosynthetic process
A	0008483	molecular_function	transaminase activity
A	0008615	biological_process	pyridoxine biosynthetic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042802	molecular_function	identical protein binding
A	0070062	cellular_component	extracellular exosome
B	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006563	biological_process	L-serine metabolic process
B	0006564	biological_process	L-serine biosynthetic process
B	0008483	molecular_function	transaminase activity
B	0008615	biological_process	pyridoxine biosynthetic process
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042802	molecular_function	identical protein binding
B	0070062	cellular_component	extracellular exosome
C	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006563	biological_process	L-serine metabolic process
C	0006564	biological_process	L-serine biosynthetic process
C	0008483	molecular_function	transaminase activity
C	0008615	biological_process	pyridoxine biosynthetic process
C	0030170	molecular_function	pyridoxal phosphate binding
C	0042802	molecular_function	identical protein binding
C	0070062	cellular_component	extracellular exosome
D	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006563	biological_process	L-serine metabolic process
D	0006564	biological_process	L-serine biosynthetic process
D	0008483	molecular_function	transaminase activity
D	0008615	biological_process	pyridoxine biosynthetic process
D	0030170	molecular_function	pyridoxal phosphate binding
D	0042802	molecular_function	identical protein binding
D	0070062	cellular_component	extracellular exosome
E	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006563	biological_process	L-serine metabolic process
E	0006564	biological_process	L-serine biosynthetic process
E	0008483	molecular_function	transaminase activity
E	0008615	biological_process	pyridoxine biosynthetic process
E	0030170	molecular_function	pyridoxal phosphate binding
E	0042802	molecular_function	identical protein binding
E	0070062	cellular_component	extracellular exosome
F	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006563	biological_process	L-serine metabolic process
F	0006564	biological_process	L-serine biosynthetic process
F	0008483	molecular_function	transaminase activity
F	0008615	biological_process	pyridoxine biosynthetic process
F	0030170	molecular_function	pyridoxal phosphate binding
F	0042802	molecular_function	identical protein binding
F	0070062	cellular_component	extracellular exosome
G	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
G	0005515	molecular_function	protein binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006563	biological_process	L-serine metabolic process
G	0006564	biological_process	L-serine biosynthetic process
G	0008483	molecular_function	transaminase activity
G	0008615	biological_process	pyridoxine biosynthetic process
G	0030170	molecular_function	pyridoxal phosphate binding
G	0042802	molecular_function	identical protein binding
G	0070062	cellular_component	extracellular exosome
H	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
H	0005515	molecular_function	protein binding
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0006563	biological_process	L-serine metabolic process
H	0006564	biological_process	L-serine biosynthetic process
H	0008483	molecular_function	transaminase activity
H	0008615	biological_process	pyridoxine biosynthetic process
H	0030170	molecular_function	pyridoxal phosphate binding
H	0042802	molecular_function	identical protein binding
H	0070062	cellular_component	extracellular exosome

Functional Information from PROSITE/UniProt

site_id	PS00595
Number of Residues	20
Details	AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. FGVIfaGAQKnvgsa.GvTvV

Chain	Residue	Details
D	PHE191-VAL210
B	PHE191-VAL210

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: in other chain => ECO:0000269\|PubMed:36851825, ECO:0007744\|PDB:8A5W

Chain	Residue	Details
B	HIS44
A	ARG45
H	HIS44
H	ARG45
B	ARG45
G	HIS44
G	ARG45
C	HIS44
C	ARG45
F	HIS44
F	ARG45
A	HIS44

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|Ref.11, ECO:0000305\|PubMed:36851825, ECO:0007744\|PDB:3E77, ECO:0007744\|PDB:8A5V

Chain	Residue	Details
B	GLY79
G	THR156
G	ASP176
G	GLN199
C	GLY79
C	CYS80
C	TRP107
C	THR156
C	ASP176
C	GLN199
F	GLY79
B	CYS80
F	CYS80
F	TRP107
F	THR156
F	ASP176
F	GLN199
A	GLY79
A	CYS80
A	TRP107
A	THR156
A	ASP176
B	TRP107
A	GLN199
H	GLY79
H	CYS80
H	TRP107
H	THR156
H	ASP176
H	GLN199
B	THR156
B	ASP176
B	GLN199
G	GLY79
G	CYS80
G	TRP107

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: in other chain => ECO:0000269\|PubMed:36851825, ECO:0007744\|PDB:3E77, ECO:0007744\|PDB:8A5V

Chain	Residue	Details
B	ASN241
G	ASN241
C	ASN241
F	ASN241
A	ASN241
H	ASN241

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: in other chain => ECO:0000269\|Ref.11, ECO:0000305\|PubMed:36851825, ECO:0007744\|PDB:3E77, ECO:0007744\|PDB:8A5V

Chain	Residue	Details
B	THR242
G	THR242
C	THR242
F	THR242
A	THR242
H	THR242

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:36851825, ECO:0007744\|PDB:8A5W

Chain	Residue	Details
B	HIS335
F	HIS335
F	ARG336
F	ARG342
A	HIS335
A	ARG336
A	ARG342
H	HIS335
H	ARG336
H	ARG342
B	ARG336
B	ARG342
G	HIS335
G	ARG336
G	ARG342
C	HIS335
C	ARG336
C	ARG342

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N-acetylmethionine => ECO:0007744\|PubMed:19413330

Chain	Residue	Details
B	MET1
G	MET1
C	MET1
F	MET1
A	MET1
H	MET1

site_id	SWS_FT_FI7
Number of Residues	10
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
B	LYS51
G	LYS333
C	LYS51
C	LYS269
C	LYS318
C	LYS323
C	LYS333
F	LYS51
F	LYS269
F	LYS318
F	LYS323
B	LYS269
F	LYS333
A	LYS51
A	LYS269
A	LYS318
A	LYS323
A	LYS333
H	LYS51
H	LYS269
H	LYS318
H	LYS323
B	LYS318
H	LYS333
B	LYS323
B	LYS333
G	LYS51
G	LYS269
G	LYS318
G	LYS323

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:Q99K85

Chain	Residue	Details
B	LYS127
G	LYS127
C	LYS127
F	LYS127
A	LYS127
H	LYS127

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269\|PubMed:36851825, ECO:0000269\|Ref.11, ECO:0007744\|PDB:3E77, ECO:0007744\|PDB:8A5V

Chain	Residue	Details
B	LYS200
G	LYS200
C	LLP200
F	LLP200
A	LLP200
H	LLP200

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
B	SER331
G	SER331
C	SER331
F	SER331
A	SER331
H	SER331

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