1S5U

Crystal Structure of Hypothetical Protein EC709 from Escherichia coli

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 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)
B	d1s5ub_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	4HBT-like	Hypothetical protein YbgC	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1s5ua_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	4HBT-like	Hypothetical protein YbgC	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1s5uc_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	4HBT-like	Hypothetical protein YbgC	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d1s5ud_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	4HBT-like	Hypothetical protein YbgC	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
E	d1s5ue1	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	4HBT-like	Hypothetical protein YbgC	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
E	d1s5ue2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
F	d1s5uf_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	4HBT-like	Hypothetical protein YbgC	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
G	d1s5ug_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	4HBT-like	Hypothetical protein YbgC	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
H	d1s5uh_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	4HBT-like	Hypothetical protein YbgC	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8041397	3000149	SCOP2B (2022-06-29)
A	SCOP2 Family	4HBT-like	8029018	4001116	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8041397	3000149	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8041397	3000149	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8041397	3000149	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8041397	3000149	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8041397	3000149	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8041397	3000149	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8041397	3000149	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	4HBT_2	e1s5uB1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: 4HBT_2	ECOD (1.6)
A	4HBT_2	e1s5uA1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: 4HBT_2	ECOD (1.6)
C	4HBT_2	e1s5uC1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: 4HBT_2	ECOD (1.6)
D	4HBT_2	e1s5uD1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: 4HBT_2	ECOD (1.6)
E	4HBT_2	e1s5uE1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: 4HBT_2	ECOD (1.6)
F	4HBT_2	e1s5uF1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: 4HBT_2	ECOD (1.6)
G	4HBT_2	e1s5uG1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: 4HBT_2	ECOD (1.6)
H	4HBT_2	e1s5uH1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: 4HBT_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)
A	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)
C	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)
D	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)
E	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)
F	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)
G	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)
H	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H	PF03061	Thioesterase superfamily (4HBT)	Thioesterase superfamily	This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyses the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas ...	This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyses the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyse the hydrolysis of other long chain fatty acyl-CoA thioesters.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H	Protein ybgC	hydrolase activity, acting on ester bonds thiolester hydrolase activity hydrolase activity fatty acyl-CoA hydrolase activity catalytic activity acyl-CoA hydrolase activity	organic substance metabolic process primary metabolic process metabolic process lipid metabolic process	cell periphery plasma membrane membrane cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR014166	Tol-Pal system-associated acyl-CoA thioesterase	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR008272	4-hydroxybenzoyl-CoA thioesterase, active site	Active Site
A, B, C, D, E A, B, C, D, E, F, G, H	IPR006684	Acyl-CoA thioester hydrolase YbgC/YbaW family	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR029069	HotDog domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR006683	Thioesterase domain	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.