5X8F

Ternary complex structure of a double mutant I454RA456K of o-Succinylbenzoate CoA Synthetase (MenE) from Bacillus Subtilis bound with AMP and its product analogue OSB-NCoA at 1.76 angstrom

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5x8fa_	Multi-domain proteins (alpha and beta)	Acetyl-CoA synthetase-like	Acetyl-CoA synthetase-like	automated matches	automated matches	(Bacillus subtilis subsp. subtilis str. 168 ) [TaxId: 224308 ],	SCOPe (2.08)
B	d5x8fb_	Multi-domain proteins (alpha and beta)	Acetyl-CoA synthetase-like	Acetyl-CoA synthetase-like	automated matches	automated matches	(Bacillus subtilis subsp. subtilis str. 168 ) [TaxId: 224308 ],	SCOPe (2.08)
C	d5x8fc_	Multi-domain proteins (alpha and beta)	Acetyl-CoA synthetase-like	Acetyl-CoA synthetase-like	automated matches	automated matches	(Bacillus subtilis subsp. subtilis str. 168 ) [TaxId: 224308 ],	SCOPe (2.08)
D	d5x8fd_	Multi-domain proteins (alpha and beta)	Acetyl-CoA synthetase-like	Acetyl-CoA synthetase-like	automated matches	automated matches	(Bacillus subtilis subsp. subtilis str. 168 ) [TaxId: 224308 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00501	e5x8fA4	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
A	PF13193	e5x8fA2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: PF13193	ECOD (1.6)
A	PF00501	e5x8fA3	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
B	PF00501	e5x8fB3	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
B	PF13193	e5x8fB4	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: PF13193	ECOD (1.6)
B	PF00501	e5x8fB1	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
C	PF00501	e5x8fC4	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
C	PF13193	e5x8fC1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: PF13193	ECOD (1.6)
C	PF00501	e5x8fC3	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
D	PF00501	e5x8fD2	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
D	PF13193	e5x8fD4	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: PF13193	ECOD (1.6)
D	PF00501	e5x8fD1	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
A	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
B	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
B	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
C	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
C	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
D	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
D	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00501	AMP-binding enzyme (AMP-binding)	AMP-binding enzyme	-	Family
A, B, C, D	PF13193	AMP-binding enzyme C-terminal domain (AMP-binding_C)	AMP-binding enzyme C-terminal domain	This is a small domain that is found C terminal to Pfam:PF00501. It has a central beta sheet core that is flanked by alpha helices.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	2-succinylbenzoate--CoA ligase	CoA-ligase activity ligase activity, forming carbon-sulfur bonds catalytic activity ligase activity binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding CoA-ligase activity ligase activity, forming carbon-sulfur bonds catalytic activity ligase activity binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding o-succinylbenzoate-CoA ligase activity acid-thiol ligase activity	small molecule biosynthetic process cellular biosynthetic process cellular metabolic process cellular ketone metabolic process organic substance metabolic process biosynthetic process menaquinone metabolic process organic substance biosynthetic process small molecule metabolic process metabolic process cellular process menaquinone biosynthetic process ketone biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR020845	AMP-binding, conserved site	Conserved Site
A, B, C, D	IPR045851	AMP-binding enzyme, C-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR042099	ANL, N-terminal domain	Homologous Superfamily
A, B, C, D	IPR025110	AMP-binding enzyme, C-terminal domain	Domain
A, B, C, D	IPR000873	AMP-dependent synthetase/ligase domain	Domain
A, B, C, D	IPR010192	2-succinylbenzoate--CoA ligase	Family

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.