3TQX

Structure of the 2-amino-3-ketobutyrate coenzyme A ligase (kbl) from Coxiella burnetii

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005829	cellular_component	cytosol
A	0006567	biological_process	threonine catabolic process
A	0008890	molecular_function	glycine C-acetyltransferase activity
A	0009058	biological_process	biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0016874	molecular_function	ligase activity
A	0019518	biological_process	L-threonine catabolic process to glycine
A	0030170	molecular_function	pyridoxal phosphate binding
B	0005829	cellular_component	cytosol
B	0006567	biological_process	threonine catabolic process
B	0008890	molecular_function	glycine C-acetyltransferase activity
B	0009058	biological_process	biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0016874	molecular_function	ligase activity
B	0019518	biological_process	L-threonine catabolic process to glycine
B	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP A 397

Chain	Residue
A	SER108
A	LYS242
A	GLY249
A	HOH422
B	SER272
B	ASN273
A	CYS109
A	PHE110
A	HIS134
A	SER136
A	ASP208
A	SER210
A	HIS211
A	THR239

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site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP B 397

Chain	Residue
A	PHE271
A	SER272
A	ASN273
B	SER108
B	CYS109
B	PHE110
B	HIS134
B	ASP208
B	SER210
B	HIS211
B	THR239
B	LYS242
B	HOH484

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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. TLGKALGGAS

Chain	Residue	Details
A	THR239-SER248

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