3E77

Human phosphoserine aminotransferase in complex with PLP

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	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	0008652	biological_process	amino acid biosynthetic process
A	0016740	molecular_function	transferase activity
A	0030170	molecular_function	pyridoxal phosphate 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	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	0008652	biological_process	amino acid biosynthetic process
B	0016740	molecular_function	transferase activity
B	0030170	molecular_function	pyridoxal phosphate 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	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	0008652	biological_process	amino acid biosynthetic process
C	0016740	molecular_function	transferase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0070062	cellular_component	extracellular exosome
C	0110076	biological_process	negative regulation of ferroptosis

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP A 400

Chain	Residue
A	GLY78
A	SER179
A	GLN199
A	LYS200
A	HOH509
A	HOH582
B	ASN241
B	THR242
A	GLY79
A	CYS80
A	PHE83
A	TRP107
A	ASN154
A	THR156
A	ASP176
A	SER178

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 500

Chain	Residue
A	LEU128
A	GLY129
A	SER130
A	LYS133

---

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP B 400

Chain	Residue
A	ASN241
A	THR242
B	GLY78
B	GLY79
B	CYS80
B	TRP107
B	THR156
B	ASP176
B	SER178
B	SER179
B	GLN199
B	LYS200
B	HOH434

---

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
A	PHE191-VAL210

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
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	18
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	3
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	3
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	9
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	15
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	3
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	3
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	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1bjo

Chain	Residue	Details
A	TRP107
A	LYS200
A	ASP176

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1bjo

Chain	Residue	Details
B	TRP107
B	LYS200
B	ASP176

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1bjo

Chain	Residue	Details
C	TRP107
C	LYS200
C	ASP176

---