Annotations: 1JFL

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1jfla1	Alpha and beta proteins (a/b)	ATC-like	Aspartate/glutamate racemase	Aspartate/glutamate racemase	Aspartate racemase	(Pyrococcus horikoshii OT3 ) [TaxId: 70601 ],	SCOPe (2.08)
B	d1jflb1	Alpha and beta proteins (a/b)	ATC-like	Aspartate/glutamate racemase	Aspartate/glutamate racemase	Aspartate racemase	(Pyrococcus horikoshii OT3 ) [TaxId: 70601 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Aspartate/glutamate racemase	8027514	4000796	SCOP2 (2022-06-29)
A	SCOP2 Family	Aspartate/glutamate racemase	8027515	4000796	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Aspartate/glutamate racemase	8039893	3001414	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Aspartate/glutamate racemase	8039894	3001414	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Aspartate/glutamate racemase	8039894	3001414	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Aspartate/glutamate racemase	8039893	3001414	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	Asp_Glu_race_C	e1jflA2	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	e1jflA1	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	e1jflB2	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	e1jflB1	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	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	ASPARTATE RACEMASE	isomerase activity racemase and epimerase activity racemase and epimerase activity, acting on amino acids and derivatives amino-acid racemase activity aspartate racemase activity catalytic activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

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

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

Chains	Enzyme Name	Description	Catalytic Residues
A	aspartate racemase (CC-type) M-CSA #335	Although L-enantiomers of amino acids are predominant in living organisms, D-enantiomers are distributed widely in bacteria, archaea and mammalian tissue. D-aspartate (D-Asp) is one of the most abundant D-enantiomers. Aspartate racemase (AspR) is a pyridoxal 5'-phosphate (PLP)-independent amino acid racemase that catalyses the interconversion of L-Asp and D-Asp.	Defined by 6 residues: ARG:A-48CYS:A-82THR:A-84THR:A-124LYS:A-164CYS:A-194 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 5.1.1.13 (PDB Primary Data) Search M-CSA Motif + EC 5.1.1.13

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.