8A5W

Crystal structure of the human phosphoserine aminotransferase (PSAT) in complex with O-phosphoserine

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	0006564	biological_process	L-serine biosynthetic process
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
A	0110076	biological_process	negative regulation of ferroptosis
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	0006564	biological_process	L-serine biosynthetic process
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
B	0110076	biological_process	negative regulation of ferroptosis
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	0006564	biological_process	L-serine biosynthetic process
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
C	0110076	biological_process	negative regulation of ferroptosis
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	0006564	biological_process	L-serine biosynthetic process
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
D	0110076	biological_process	negative regulation of ferroptosis
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	0006564	biological_process	L-serine biosynthetic process
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
E	0110076	biological_process	negative regulation of ferroptosis
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	0006564	biological_process	L-serine biosynthetic process
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
F	0110076	biological_process	negative regulation of ferroptosis
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	0006564	biological_process	L-serine biosynthetic process
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
G	0110076	biological_process	negative regulation of ferroptosis
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	0006564	biological_process	L-serine biosynthetic process
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
H	0110076	biological_process	negative regulation of ferroptosis

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
E	PHE191-VAL210
D	PHE191-VAL210

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"36851825","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8A5W","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2008","submissionDatabase":"PDB data bank","title":"Human phosphoserine aminotransferase in complex with PLP.","authoringGroup":["Structural Genomics Consortium (SGC)"],"authors":["Lehtio L.","Karlberg T.","Andersson J.","Arrowsmith C.H.","Berglund H.","Bountra C.","Collins R.","Dahlgren L.G.","Edwards A.M.","Flodin S.","Flores A.","Graslund S.","Hammarstrom M.","Johansson A.","Johansson I.","Kotenyova T.","Moche M.","Nilsson M.E.","Nordlund P.","Nyman T.","Olesen K.","Persson C.","Sagemark J.","Thorsell S.G.","Tresaugues L.","Van Den Berg S.","Welin M.","Wikstrom M.","Wisniewska M.","Weigelt J.","Schueler H."]}},{"source":"PubMed","id":"36851825","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3E77","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8A5V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"36851825","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3E77","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8A5V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"description":"in other chain","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2008","submissionDatabase":"PDB data bank","title":"Human phosphoserine aminotransferase in complex with PLP.","authoringGroup":["Structural Genomics Consortium (SGC)"],"authors":["Lehtio L.","Karlberg T.","Andersson J.","Arrowsmith C.H.","Berglund H.","Bountra C.","Collins R.","Dahlgren L.G.","Edwards A.M.","Flodin S.","Flores A.","Graslund S.","Hammarstrom M.","Johansson A.","Johansson I.","Kotenyova T.","Moche M.","Nilsson M.E.","Nordlund P.","Nyman T.","Olesen K.","Persson C.","Sagemark J.","Thorsell S.G.","Tresaugues L.","Van Den Berg S.","Welin M.","Wikstrom M.","Wisniewska M.","Weigelt J.","Schueler H."]}},{"source":"PubMed","id":"36851825","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3E77","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8A5V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"36851825","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8A5W","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	40
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99K85","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	8
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"36851825","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2008","submissionDatabase":"PDB data bank","title":"Human phosphoserine aminotransferase in complex with PLP.","authoringGroup":["Structural Genomics Consortium (SGC)"],"authors":["Lehtio L.","Karlberg T.","Andersson J.","Arrowsmith C.H.","Berglund H.","Bountra C.","Collins R.","Dahlgren L.G.","Edwards A.M.","Flodin S.","Flores A.","Graslund S.","Hammarstrom M.","Johansson A.","Johansson I.","Kotenyova T.","Moche M.","Nilsson M.E.","Nordlund P.","Nyman T.","Olesen K.","Persson C.","Sagemark J.","Thorsell S.G.","Tresaugues L.","Van Den Berg S.","Welin M.","Wikstrom M.","Wisniewska M.","Weigelt J.","Schueler H."]}},{"source":"PDB","id":"3E77","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8A5V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine; by CAMK2A","evidences":[{"source":"PubMed","id":"40281343","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---