5DPM

Crystal structure of UbiG mutant in complex with SAH

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006744	biological_process	ubiquinone biosynthetic process
A	0008168	molecular_function	methyltransferase activity
A	0008425	molecular_function	2-methoxy-6-polyprenyl-1,4-benzoquinol methyltransferase activity
A	0009898	cellular_component	cytoplasmic side of plasma membrane
A	0010420	molecular_function	polyprenyldihydroxybenzoate methyltransferase activity
A	0016740	molecular_function	transferase activity
A	0032259	biological_process	methylation
A	0042538	biological_process	hyperosmotic salinity response
A	0061542	molecular_function	3-demethylubiquinol 3-O-methyltransferase activity
A	0102208	molecular_function	2-polyprenyl-6-hydroxyphenol methylase activity
A	0110142	cellular_component	ubiquinone biosynthesis complex
A	1901611	molecular_function	phosphatidylglycerol binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue SAH A 301

Chain	Residue
A	ASN11
A	MET86
A	MET129
A	GLU130
A	MET131
A	HOH408
A	HOH420
A	HOH423
A	HOH446
A	PHE20
A	TRP27
A	LEU37
A	ARG44
A	GLY64
A	CYS65
A	GLY66
A	ASP85

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00472","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2013","submissionDatabase":"PDB data bank","title":"Crystal structure of the UbiG/SAH complex.","authors":["Zhu Y.","Teng M.","Li X."]}}]}

Chain

Residue

Details

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