6VL1

Crystal Structure of the N-prenyltransferase DabA in Complex with NGG and Mg2+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016036	biological_process	cellular response to phosphate starvation
A	0016740	molecular_function	transferase activity
A	0046872	molecular_function	metal ion binding
A	0071244	biological_process	cellular response to carbon dioxide

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue MG A 601

Chain	Residue
A	ASP352
A	GLU359
A	PHE366
A	R1V602
A	HOH723
A	HOH736
A	HOH801

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site_id	AC2
Number of Residues	19
Details	binding site for residue R1V A 602

Chain	Residue
A	TYR163
A	MET166
A	TYR167
A	ASN170
A	ARG306
A	THR310
A	ILE347
A	ASN351
A	ARG358
A	GLU359
A	ARG447
A	MG601
A	HOH723
A	HOH801
A	HOH826
A	HOH889
A	HOH911
A	THR143
A	CYS147

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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":"32457155","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6VKZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6VL0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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