2VSS

Wild-type Hydroxycinnamoyl-CoA hydratase lyase in complex with acetyl- CoA and vanillin

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2vssa_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Pseudomonas fluorescens ) [TaxId: 294 ],	SCOPe (2.08)
B	d2vssb_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Pseudomonas fluorescens ) [TaxId: 294 ],	SCOPe (2.08)
C	d2vssc_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Pseudomonas fluorescens ) [TaxId: 294 ],	SCOPe (2.08)
D	d2vssd_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Pseudomonas fluorescens ) [TaxId: 294 ],	SCOPe (2.08)
E	d2vsse_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Pseudomonas fluorescens ) [TaxId: 294 ],	SCOPe (2.08)
F	d2vssf_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Pseudomonas fluorescens ) [TaxId: 294 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	ClpP/crotonase	8067193	3000033	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	ClpP/crotonase	8067193	3000033	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	ClpP/crotonase	8067193	3000033	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	ClpP/crotonase	8067193	3000033	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	ClpP/crotonase	8067193	3000033	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	ClpP/crotonase	8067193	3000033	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)
A	PF00378	e2vssA1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: PF00378	ECOD (1.6)
B	PF00378	e2vssB1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: PF00378	ECOD (1.6)
C	PF00378	e2vssC1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: PF00378	ECOD (1.6)
D	PF00378	e2vssD1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: PF00378	ECOD (1.6)
E	PF00378	e2vssE1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: PF00378	ECOD (1.6)
F	PF00378	e2vssF1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: PF00378	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
A	6.10.250.2850	Special	Helix non-globular	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)
B	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
B	6.10.250.2850	Special	Helix non-globular	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)
C	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
C	6.10.250.2850	Special	Helix non-globular	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)
D	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
D	6.10.250.2850	Special	Helix non-globular	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)
E	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
E	6.10.250.2850	Special	Helix non-globular	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)
F	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
F	6.10.250.2850	Special	Helix non-globular	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00378	Enoyl-CoA hydratase/isomerase (ECH_1)	Enoyl-CoA hydratase/isomerase	This family contains a diverse set of enzymes including: enoyl-CoA hydratase, napthoate synthase, carnitate racemase, 3-hydroxybutyryl-CoA dehydratase and dodecanoyl-CoA delta-isomerase.	Domain
E	PF00378	Enoyl-CoA hydratase/isomerase (ECH_1)	Enoyl-CoA hydratase/isomerase	This family contains a diverse set of enzymes including: enoyl-CoA hydratase, napthoate synthase, carnitate racemase, 3-hydroxybutyryl-CoA dehydratase and dodecanoyl-CoA delta-isomerase.	Domain
F	PF00378	Enoyl-CoA hydratase/isomerase (ECH_1)	Enoyl-CoA hydratase/isomerase	This family contains a diverse set of enzymes including: enoyl-CoA hydratase, napthoate synthase, carnitate racemase, 3-hydroxybutyryl-CoA dehydratase and dodecanoyl-CoA delta-isomerase.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	P-HYDROXYCINNAMOYL COA HYDRATASE/LYASE	trans-feruloyl-CoA hydratase activity hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity vanillin synthase activity carbon-carbon lyase activity aldehyde-lyase activity	-	-
E	P-HYDROXYCINNAMOYL COA HYDRATASE/LYASE	trans-feruloyl-CoA hydratase activity hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity vanillin synthase activity carbon-carbon lyase activity aldehyde-lyase activity	-	-
F	P-HYDROXYCINNAMOYL COA HYDRATASE/LYASE	trans-feruloyl-CoA hydratase activity hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity vanillin synthase activity carbon-carbon lyase activity aldehyde-lyase activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR001753	Enoyl-CoA hydratase/isomerase	Family
A, B, C, D	IPR029045	ClpP/crotonase-like domain superfamily	Homologous Superfamily
A, B, C, D	IPR018376	Enoyl-CoA hydratase/isomerase, conserved site	Conserved Site
E	IPR001753	Enoyl-CoA hydratase/isomerase	Family
E	IPR029045	ClpP/crotonase-like domain superfamily	Homologous Superfamily
E	IPR018376	Enoyl-CoA hydratase/isomerase, conserved site	Conserved Site
F	IPR001753	Enoyl-CoA hydratase/isomerase	Family
F	IPR029045	ClpP/crotonase-like domain superfamily	Homologous Superfamily
F	IPR018376	Enoyl-CoA hydratase/isomerase, conserved site	Conserved Site

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A, B	feruloyl CoA hydratase/lyase M-CSA #347	Catalyses the hydration of the acyl-CoA thioester of ferulic acid and the subsequent retro-aldol cleavage of the hydrated intermediate to yield vanillin (4-hydroxy-3-methoxy-benzaldehyde) and acetyl-CoA. This is a member of the crotonase superfamily.	Defined by 5 residues: MET:A-70TYR:A-75GLY:A-120GLU:A-143TYR:B-239 Some residues are not modelled and lack atomic coordinates. Visualization is not available. Some residues are not modelled and lack atomic coordinates. Structure Motif searching is not available. EC: 4.2.1.101 (PDB Primary Data)

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.