1R6W

Crystal structure of the K133R mutant of o-Succinylbenzoate synthase (OSBS) from Escherichia coli. Complex with SHCHC

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	5
Details	BINDING SITE FOR RESIDUE MG A 736

Chain	Residue
A	ASP161
A	GLU190
A	ASP213
A	164735
A	HOH1073

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site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 164 A 735

Chain	Residue
A	GLU190
A	ASP213
A	LYS235
A	SER262
A	SER263
A	GLY288
A	MG736
A	HOH738
A	HOH773
A	HOH796
A	HOH1073
A	PHE51
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	ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000269|PubMed:10978150

Chain	Residue	Details
A	ARG133

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000269|PubMed:10978150

Chain	Residue	Details
A	LYS235

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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:10978150

Chain	Residue	Details
A	ASP161
A	GLU190
A	ASP213

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 14661953

Chain	Residue	Details
A	ARG133
A	LYS235

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 689

Chain	Residue	Details
A	ARG133	proton acceptor, proton donor
A	ASP161	metal ligand
A	GLU190	metal ligand
A	ASP213	metal ligand
A	LYS235	electrostatic stabiliser

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