3C20

Crystal Structure of Threonine-sensitive Aspartokinase from Methanococcus jannaschii with L-aspartate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004072	molecular_function	aspartate kinase activity
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0008652	biological_process	amino acid biosynthetic process
A	0009088	biological_process	threonine biosynthetic process
A	0009089	biological_process	lysine biosynthetic process via diaminopimelate
A	0009090	biological_process	homoserine biosynthetic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
B	0000166	molecular_function	nucleotide binding
B	0004072	molecular_function	aspartate kinase activity
B	0005524	molecular_function	ATP binding
B	0005829	cellular_component	cytosol
B	0008652	biological_process	amino acid biosynthetic process
B	0009088	biological_process	threonine biosynthetic process
B	0009089	biological_process	lysine biosynthetic process via diaminopimelate
B	0009090	biological_process	homoserine biosynthetic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ASP B 474

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ASP A 474

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 475

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT B 475

Functional Information from PROSITE/UniProt

site_id	PS00324
Number of Residues	9
Details	ASPARTOKINASE Aspartokinase signature. VmKFGGTSV

Chain	Residue	Details
A	VAL4-VAL12