2JG2

HIGH RESOLUTION STRUCTURE OF SPT WITH PLP INTERNAL ALDIMINE

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP A 1265

Chain	Residue
A	GLY134
A	SER264
A	LYS265
A	GLY271
A	THR294
A	ALA295
A	HOH2290
A	TYR135
A	ASN138
A	HIS159
A	SER161
A	GLU202
A	ASP231
A	HIS234
A	THR262

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1421

Chain	Residue
A	HOH2030
A	HOH2062
A	HOH2064
A	HOH2102
A	HOH2104

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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	3
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

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:17559874, ECO:0007744|PDB:2JG2

Chain	Residue	Details
A	HIS234

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site_id	SWS_FT_FI3
Number of Residues	1
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

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