1FHV

CRYSTAL STRUCTURE ANALYSIS OF O-SUCCINYLBENZOATE SYNTHASE FROM E. COLI COMPLEXED WITH MG AND OSB

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	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 790

Chain	Residue
A	ASP161
A	GLU190
A	ASP213
A	HOH592
A	HOH674
A	OSB789

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site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE OSB A 789

Chain	Residue
A	ASP213
A	LYS235
A	SER262
A	SER263
A	GLY288
A	HOH674
A	HOH742
A	HOH779
A	HOH785
A	MG790
A	LYS131
A	ASP161
A	ASN163

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00470","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10978150","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00470","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10978150","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00470","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10978150","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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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	LYS133
A	LYS235

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 689

Chain	Residue	Details
A	LYS133	proton acceptor, proton donor
A	ASP161	metal ligand
A	GLU190	metal ligand
A	ASP213	metal ligand
A	LYS235	electrostatic stabiliser

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