3WQD

D-threo-3-hydroxyaspartate dehydratase from Delftia sp. HT23 complexed with D-erythro-3-hydroxyaspartate

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	D-ser_dehydrat	e3wqdB2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: D-ser_dehydrat	ECOD (1.6)
B	Ala_racemase_N	e3wqdB1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Ala_racemase_N	ECOD (1.6)
A	D-ser_dehydrat	e3wqdA2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: D-ser_dehydrat	ECOD (1.6)
A	Ala_racemase_N	e3wqdA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Ala_racemase_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	2.40.37.20	Mainly Beta	Beta Barrel	Lyase, Ornithine Decarboxylase	Chain A, domain 1	CATH (4.3.0)
B	3.20.20.10	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Alanine racemase	CATH (4.3.0)
A	2.40.37.20	Mainly Beta	Beta Barrel	Lyase, Ornithine Decarboxylase	Chain A, domain 1	CATH (4.3.0)
A	3.20.20.10	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Alanine racemase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF14031	Putative serine dehydratase domain (D-ser_dehydrat)	Putative serine dehydratase domain	This domain is found at the C-terminus of yeast D-serine dehydratase [1]. Structures have been solved for two bacterial members of this family. The yeast protein has been shown to be a zinc dependant enzyme.	Domain
A, B	PF01168	Alanine racemase, N-terminal domain (Ala_racemase_N)	Alanine racemase, N-terminal domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	D-threo-3-hydroxyaspartate dehydratase	lyase activity ammonia-lyase activity catalytic activity carbon-nitrogen lyase activity vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding binding organic cyclic compound binding anion binding heterocyclic compound binding small molecule binding D-serine ammonia-lyase activity	catabolic process oxoacid metabolic process non-proteinogenic amino acid catabolic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process organic acid catabolic process D-serine metabolic process alpha-amino acid metabolic process cellular catabolic process non-proteinogenic amino acid metabolic process alpha-amino acid catabolic process carboxylic acid catabolic process D-amino acid metabolic process catabolic process oxoacid metabolic process non-proteinogenic amino acid catabolic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process organic acid catabolic process D-serine metabolic process alpha-amino acid metabolic process cellular catabolic process non-proteinogenic amino acid metabolic process alpha-amino acid catabolic process carboxylic acid catabolic process D-amino acid metabolic process metabolic process cellular process small molecule metabolic process small molecule catabolic process D-amino acid catabolic process amino acid catabolic process D-serine catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR029066	PLP-binding barrel	Homologous Superfamily
A, B	IPR042208	D-serine dehydratase-like domain superfamily	Homologous Superfamily
A, B	IPR026956	D-serine dehydratase-like domain	Domain
A, B	IPR051466	D-amino acid metabolism enzyme	Family
A, B	IPR001608	Alanine racemase, N-terminal	Domain

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.