2JGT

Low resolution structure of SPT

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0006629	biological_process	lipid metabolic process
A	0006665	biological_process	sphingolipid metabolic process
A	0009058	biological_process	biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
B	0005737	cellular_component	cytoplasm
B	0006629	biological_process	lipid metabolic process
B	0006665	biological_process	sphingolipid metabolic process
B	0009058	biological_process	biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PROSITE/UniProt

site_id	PS00599
Number of Residues	10
Details	AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TFSKSVGTVG

Chain	Residue	Details
A	THR262-GLY271

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:17559874, ECO:0000269|PubMed:19376777, ECO:0007744|PDB:2JG2, ECO:0007744|PDB:2W8T, ECO:0007744|PDB:2W8U, ECO:0007744|PDB:2W8V

Chain	Residue	Details
A	GLY134
A	THR262
A	SER264
B	GLY134
B	THR262
B	SER264

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:17559874, ECO:0007744|PDB:2JG2

Chain	Residue	Details
A	HIS234
B	HIS234

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:17559874, ECO:0000269|PubMed:19376777, ECO:0007744|PDB:2JG2, ECO:0007744|PDB:2W8T, ECO:0007744|PDB:2W8U, ECO:0007744|PDB:2W8V

Chain	Residue	Details
A	LYS265
B	LYS265

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