Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1SJA

X-ray structure of o-Succinylbenzoate Synthase complexed with N-acetylmethionine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0009234	biological_process	menaquinone biosynthetic process
A	0016829	molecular_function	lyase activity
A	0016853	molecular_function	isomerase activity
A	0043748	molecular_function	O-succinylbenzoate synthase activity
A	0046872	molecular_function	metal ion binding
B	0003824	molecular_function	catalytic activity
B	0009234	biological_process	menaquinone biosynthetic process
B	0016829	molecular_function	lyase activity
B	0016853	molecular_function	isomerase activity
B	0043748	molecular_function	O-succinylbenzoate synthase activity
B	0046872	molecular_function	metal ion binding
C	0003824	molecular_function	catalytic activity
C	0009234	biological_process	menaquinone biosynthetic process
C	0016829	molecular_function	lyase activity
C	0016853	molecular_function	isomerase activity
C	0043748	molecular_function	O-succinylbenzoate synthase activity
C	0046872	molecular_function	metal ion binding
D	0003824	molecular_function	catalytic activity
D	0009234	biological_process	menaquinone biosynthetic process
D	0016829	molecular_function	lyase activity
D	0016853	molecular_function	isomerase activity
D	0043748	molecular_function	O-succinylbenzoate synthase activity
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG A 601

Chain	Residue
A	ASP189
A	ASN191
A	GLU214
A	ASP239
A	GLU240
A	AME600
A	HOH673

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE AME A 600

Chain	Residue
A	SER135
A	LYS161
A	LYS163
A	ASP189
A	GLU214
A	ASP239
A	LYS263
A	GLY291
A	MET292
A	ASP316
A	MG601
A	HOH695
A	PHE23
A	MET50

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 701

Chain	Residue
B	ASP189
B	ASN191
B	GLU214
B	ASP239
B	AME700
B	HOH775

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE AME B 700

Chain	Residue
B	PHE19
B	PHE23
B	MET50
B	SER135
B	LYS161
B	LYS163
B	ASP189
B	GLU214
B	ASP239
B	ASN261
B	LYS263
B	GLY291
B	ASP316
B	MG701

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 801

Chain	Residue
C	ASP189
C	ASN191
C	GLU214
C	ASP239
C	AME800
C	HOH871

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE AME C 800

Chain	Residue
C	MET50
C	SER135
C	LYS161
C	LYS163
C	ASP189
C	GLU214
C	ASP239
C	LYS263
C	GLY291
C	MET292
C	ILE293
C	ASP316
C	MG801
C	HOH895

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG D 901

Chain	Residue
D	ASP189
D	ASN191
D	GLU214
D	ASP239
D	GLU240
D	AME900
D	HOH970

site_id	AC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AME D 900

Chain	Residue
D	PHE19
D	PHE23
D	MET50
D	SER135
D	LYS161
D	LYS163
D	ASP189
D	ASN191
D	GLU214
D	ASP239
D	LYS263
D	GLY291
D	ASP316
D	MG901
D	HOH1000

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000305\|PubMed:14705949, ECO:0000305\|PubMed:15134446

Chain	Residue	Details
A	LYS163
B	LYS163
C	LYS163
D	LYS163

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000305\|PubMed:14705949, ECO:0000305\|PubMed:15134446

Chain	Residue	Details
A	LYS263
B	LYS263
C	LYS263
D	LYS263

site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:15134446, ECO:0007744\|PDB:1SJB

Chain	Residue	Details
A	SER135
C	LYS161
C	ASN191
C	ILE293
D	SER135
D	LYS161
D	ASN191
D	ILE293
A	LYS161
A	ASN191
A	ILE293
B	SER135
B	LYS161
B	ASN191
B	ILE293
C	SER135

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:15134446, ECO:0000269\|PubMed:23130969, ECO:0000269\|Ref.9, ECO:0007744\|PDB:1SJA, ECO:0007744\|PDB:1SJB, ECO:0007744\|PDB:1SJC, ECO:0007744\|PDB:4A6G, ECO:0007744\|PDB:5FJO, ECO:0007744\|PDB:5FJP, ECO:0007744\|PDB:5FJR, ECO:0007744\|PDB:5FJT, ECO:0007744\|PDB:5FJU

Chain	Residue	Details
A	ASP189
D	ASP189
D	GLU214
D	ASP239
A	GLU214
A	ASP239
B	ASP189
B	GLU214
B	ASP239
C	ASP189
C	GLU214
C	ASP239

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1muc

Chain	Residue	Details
A	ASP316
A	LYS161
A	LYS163

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1muc

Chain	Residue	Details
B	ASP316
B	LYS161
B	LYS163

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1muc

Chain	Residue	Details
C	ASP316
C	LYS161
C	LYS163

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1muc

Chain	Residue	Details
D	ASP316
D	LYS161
D	LYS163

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1muc

Chain	Residue	Details
A	LYS161
A	LYS263

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1muc

Chain	Residue	Details
B	LYS161
B	LYS263

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1muc

Chain	Residue	Details
C	LYS161
C	LYS263

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1muc

Chain	Residue	Details
D	LYS161
D	LYS263

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1muc

Chain	Residue	Details
A	LYS263
A	LYS163

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1muc

Chain	Residue	Details
B	LYS263
B	LYS163

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1muc

Chain	Residue	Details
C	LYS263
C	LYS163

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1muc

Chain	Residue	Details
D	LYS263
D	LYS163

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)