3WWM

Crystal structure of LysZ from Thermus thermophilus with ADP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0008652	biological_process	amino acid biosynthetic process
A	0009085	biological_process	lysine biosynthetic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
A	0043744	molecular_function	N2-acetyl-L-aminoadipate kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ADP A 301

Chain	Residue
A	LYS5
A	ARG230
A	HOH401
A	HOH427
A	GLY7
A	GLY8
A	GLY36
A	GLY37
A	SER38
A	TYR78
A	TYR200
A	MET228

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25392000","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3WWM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02082","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_02082","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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