2OFJ

Crystal structure of the E190A mutant of o-succinylbenzoate synthase from Escherichia coli

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
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0009234	biological_process	menaquinone biosynthetic process
B	0016829	molecular_function	lyase activity
B	0016836	molecular_function	hydro-lyase activity
B	0043748	molecular_function	O-succinylbenzoate synthase activity
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0009234	biological_process	menaquinone biosynthetic process
C	0016829	molecular_function	lyase activity
C	0016836	molecular_function	hydro-lyase activity
C	0043748	molecular_function	O-succinylbenzoate synthase activity
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0009234	biological_process	menaquinone biosynthetic process
D	0016829	molecular_function	lyase activity
D	0016836	molecular_function	hydro-lyase activity
D	0043748	molecular_function	O-succinylbenzoate synthase activity
D	0046872	molecular_function	metal ion binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000269|PubMed:10978150

Chain	Residue	Details
A	LYS133
B	LYS133
C	LYS133
D	LYS133

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000269|PubMed:10978150

Chain	Residue	Details
A	LYS235
B	LYS235
C	LYS235
D	LYS235

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000269|PubMed:10978150

Chain	Residue	Details
A	ASP161
D	ASP161
D	ALA190
D	ASP213
A	ALA190
A	ASP213
B	ASP161
B	ALA190
B	ASP213
C	ASP161
C	ALA190
C	ASP213

---

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

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1r6w

Chain	Residue	Details
B	LYS133
B	LYS235

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1r6w

Chain	Residue	Details
C	LYS133
C	LYS235

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1r6w

Chain	Residue	Details
D	LYS133
D	LYS235

---

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	ALA190	metal ligand
A	ASP213	metal ligand
A	LYS235	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	5
Details	M-CSA 689

Chain	Residue	Details
B	LYS133	proton acceptor, proton donor
B	ASP161	metal ligand
B	ALA190	metal ligand
B	ASP213	metal ligand
B	LYS235	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	5
Details	M-CSA 689

Chain	Residue	Details
C	LYS133	proton acceptor, proton donor
C	ASP161	metal ligand
C	ALA190	metal ligand
C	ASP213	metal ligand
C	LYS235	electrostatic stabiliser

---

site_id	MCSA4
Number of Residues	5
Details	M-CSA 689

Chain	Residue	Details
D	LYS133	proton acceptor, proton donor
D	ASP161	metal ligand
D	ALA190	metal ligand
D	ASP213	metal ligand
D	LYS235	electrostatic stabiliser

---