3U6U

Crystal structure of the putative acetylglutamate kinase from thermus thermophilus

Replaces:  2EGX

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003991	molecular_function	acetylglutamate kinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006526	biological_process	L-arginine biosynthetic process
A	0009085	biological_process	lysine biosynthetic process
A	0016301	molecular_function	kinase activity
A	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
A	0043744	molecular_function	N2-acetyl-L-aminoadipate kinase activity
C	0003991	molecular_function	acetylglutamate kinase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006526	biological_process	L-arginine biosynthetic process
C	0009085	biological_process	lysine biosynthetic process
C	0016301	molecular_function	kinase activity
C	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
C	0043744	molecular_function	N2-acetyl-L-aminoadipate kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 270

Chain	Residue
A	LYS5
A	GLY8
A	GLY36
A	GLY37
A	SER38
A	TYR78
A	SO4271
A	HOH350

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 271

Chain	Residue
A	GLY8
A	ALA9
A	SER191
A	SO4270
A	HOH299
A	GLY7

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site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 C 270

Chain	Residue
C	LYS5
C	GLY8
C	GLY36
C	GLY37
C	SER38
C	TYR78
C	SO4271
C	HOH339

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site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 271

Chain	Residue
C	GLY7
C	GLY8
C	ALA9
C	SER191
C	SO4270
C	HOH279

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