3H7V

CRYSTAL STRUCTURE OF O-SUCCINYLBENZOATE SYNTHASE FROM THERMOSYNECHOCOCCUS ELONGATUS BP-1 complexed with MG in the active site

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0009234	biological_process	menaquinone biosynthetic process
A	0016829	molecular_function	lyase activity
A	0016836	molecular_function	hydro-lyase activity
A	0042372	biological_process	phylloquinone biosynthetic process
A	0043748	molecular_function	O-succinylbenzoate synthase activity
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 331

Chain	Residue
A	ASP165
A	GLU194
A	ASP219
A	HOH379
A	HOH382
A	HOH425

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00470

Chain	Residue	Details
A	LYS136

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00470

Chain	Residue	Details
A	LYS243

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site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000269|PubMed:24872444, ECO:0007744|PDB:3H7V

Chain	Residue	Details
A	ASP165
A	GLU194
A	ASP219

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1r6w

Chain	Residue	Details
A	LYS136
A	LYS243

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