2HXT

Crystal structure of L-Fuconate Dehydratase from Xanthomonas campestris liganded with Mg++ and D-erythronohydroxamate

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Enolase N-terminal domain-like	8044304	3001064	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Enolase C-terminal domain-like	8044303	3000476	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	MR_MLE_N	e2hxtA4	A: a+b two layers	X: Enolase-N/ribosomal protein	H: Enolase N-terminal domain-like (From Topology)	T: Enolase N-terminal domain-like	F: MR_MLE_N	ECOD (1.6)
A	MR_MLE_C_1	e2hxtA3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: MR_MLE_C_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.390.10	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (4.3.0)
A	3.20.20.120	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Enolase-like C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF02746	Mandelate racemase / muconate lactonizing enzyme, N-terminal domain (MR_MLE_N)	Mandelate racemase / muconate lactonizing enzyme, N-terminal domain	SCOP reports fold similarity with enolase N-terminal domain.	Domain
A	PF13378	Enolase C-terminal domain-like (MR_MLE_C)	Enolase C-terminal domain-like	This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N Pfam:PF02746 domain. EC:4.2.1.40.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	L-fuconate dehydratase	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity L-fuconate dehydratase activity	carbohydrate metabolic process catabolic process carbohydrate catabolic process primary metabolic process metabolic process cellular process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR029065	Enolase C-terminal domain-like	Domain
A	IPR013341	Mandelate racemase/muconate lactonizing enzyme, N-terminal domain	Domain
A	IPR046945	L-rhamnonate dehydratase-like	Family
A	IPR013342	Mandelate racemase/muconate lactonizing enzyme, C-terminal	Domain
A	IPR029017	Enolase-like, N-terminal	Homologous Superfamily
A	IPR034610	L-fuconate dehydratase	Family
A	IPR036849	Enolase-like, C-terminal domain superfamily	Homologous Superfamily

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

Chains	Enzyme Name	Description	Catalytic Residues
A	L-fuconate dehydratase M-CSA #961	L-fuconate dehydratase is a member of the enolase superfamily and is known to play a role in the catabolism of L-fucose. It catalyses the dehydration of L-fuconate to 2-keto-3-deoxy-L-fuconate by the abstraction of the proton alpha to the carboxylate group of the substrate to generate an enediolate intermediate that is stabilised by an essential magnesium ion.	Defined by 6 residues: LYS:A-220ASP:A-248GLU:A-274GLU:A-301ASP:A-324HIS:A-351 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 4.2.1.68 (UniProt) Search M-CSA Motif + EC 4.2.1.68

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 R01GM157729.