4AB7

Crystal structure of a tetrameric acetylglutamate kinase from Saccharomyces cerevisiae complexed with its substrate N- acetylglutamate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003991	molecular_function	acetylglutamate kinase activity
A	0005737	cellular_component	cytoplasm
A	0006526	biological_process	L-arginine biosynthetic process
B	0003991	molecular_function	acetylglutamate kinase activity
B	0005737	cellular_component	cytoplasm
B	0006526	biological_process	L-arginine biosynthetic process
C	0003991	molecular_function	acetylglutamate kinase activity
C	0005737	cellular_component	cytoplasm
C	0006526	biological_process	L-arginine biosynthetic process
D	0003991	molecular_function	acetylglutamate kinase activity
D	0005737	cellular_component	cytoplasm
D	0006526	biological_process	L-arginine biosynthetic process
E	0003991	molecular_function	acetylglutamate kinase activity
E	0005737	cellular_component	cytoplasm
E	0006526	biological_process	L-arginine biosynthetic process
F	0003991	molecular_function	acetylglutamate kinase activity
F	0005737	cellular_component	cytoplasm
F	0006526	biological_process	L-arginine biosynthetic process
G	0003991	molecular_function	acetylglutamate kinase activity
G	0005737	cellular_component	cytoplasm
G	0006526	biological_process	L-arginine biosynthetic process
H	0003991	molecular_function	acetylglutamate kinase activity
H	0005737	cellular_component	cytoplasm
H	0006526	biological_process	L-arginine biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE NLG D 1503

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE NLG H 1503

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:17330950