3OJC

Crystal structure of a putative Asp/Glu Racemase from Yersinia pestis

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	d3ojca1	Alpha and beta proteins (a/b)	ATC-like	Aspartate/glutamate racemase	automated matches	automated matches	(Yersinia pestis CO92 ) [TaxId: 214092 ],	SCOPe (2.08)
B	d3ojcb1	Alpha and beta proteins (a/b)	ATC-like	Aspartate/glutamate racemase	automated matches	automated matches	(Yersinia pestis CO92 ) [TaxId: 214092 ],	SCOPe (2.08)
C	d3ojcc1	Alpha and beta proteins (a/b)	ATC-like	Aspartate/glutamate racemase	automated matches	automated matches	(Yersinia pestis CO92 ) [TaxId: 214092 ],	SCOPe (2.08)
D	d3ojcd1	Alpha and beta proteins (a/b)	ATC-like	Aspartate/glutamate racemase	automated matches	automated matches	(Yersinia pestis CO92 ) [TaxId: 214092 ],	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	Asp_Glu_race_C	e3ojcA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: Asp_Glu_race_C	ECOD (1.6)
A	Asp_Glu_race_N	e3ojcA2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: Asp_Glu_race_N	ECOD (1.6)
B	Asp_Glu_race_C	e3ojcB2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: Asp_Glu_race_C	ECOD (1.6)
B	Asp_Glu_race_N	e3ojcB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: Asp_Glu_race_N	ECOD (1.6)
C	Asp_Glu_race_C	e3ojcC2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: Asp_Glu_race_C	ECOD (1.6)
C	Asp_Glu_race_N	e3ojcC1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: Asp_Glu_race_N	ECOD (1.6)
D	Asp_Glu_race_C	e3ojcD2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: Asp_Glu_race_C	ECOD (1.6)
D	Asp_Glu_race_N	e3ojcD1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: Asp_Glu_race_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1860	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
B	3.40.50.1860	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
C	3.40.50.1860	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
D	3.40.50.1860	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF01177	Asp/Glu/Hydantoin racemase (Asp_Glu_race)	Asp/Glu/Hydantoin racemase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Putative aspartate/glutamate racemase	racemase activity, acting on amino acids and derivatives isomerase activity racemase and epimerase activity racemase and epimerase activity, acting on amino acids and derivatives amino-acid racemase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR018187	Asp/Glu racemase, active site 1	Active Site
A, B, C, D	IPR001920	Asp/Glu racemase	Homologous Superfamily
A, B, C, D	IPR004380	Aspartate racemase	Family
A, B, C, D	IPR015942	Asp/Glu/hydantoin racemase	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 R01GM157729.