Annotations: 2V8D

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Bacterial exopeptidase dimerisation domain	8040322	3001194	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Zn-dependent exopeptidases	8040321	3000662	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Zn-dependent exopeptidases	8040321	3000662	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Zn-dependent exopeptidases	8040321	3000662	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Zn-dependent exopeptidases	8040321	3000662	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Bacterial exopeptidase dimerisation domain	8040322	3001194	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)
B	M20_dimer	e2v8dB1	A: a+b two layers	X: Alpha-beta plaits	H: Bacterial exopeptidase dimerisation domain (From Topology)	T: Bacterial exopeptidase dimerisation domain	F: M20_dimer	ECOD (1.6)
B	Peptidase_M28	e2v8dB3	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: Peptidase_M28	ECOD (1.6)
A	M20_dimer	e2v8dA1	A: a+b two layers	X: Alpha-beta plaits	H: Bacterial exopeptidase dimerisation domain (From Topology)	T: Bacterial exopeptidase dimerisation domain	F: M20_dimer	ECOD (1.6)
A	Peptidase_M28	e2v8dA3	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: Peptidase_M28	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
B	3.30.70.360	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
A	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
A	3.30.70.360	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01546	Peptidase family M20/M25/M40 (Peptidase_M20)	Peptidase family M20/M25/M40	-	Family
A, B	PF07687	Peptidase dimerisation domain (M20_dimer)	Peptidase dimerisation domain	This domain consists of 4 beta strands and two alpha helices which make up the dimerisation surface of members of the M20 family of peptidases [1]. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase ...	This domain consists of 4 beta strands and two alpha helices which make up the dimerisation surface of members of the M20 family of peptidases [1]. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification [2]. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	BETA-ALANINE SYNTHASE	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds cation binding ion binding binding metal ion binding small molecule binding beta-ureidopropionase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR002933	Peptidase M20	Family
A, B	IPR010158	Amidase, carbamoylase-type	Family
A, B	IPR036264	Bacterial exopeptidase dimerisation domain	Homologous Superfamily
A, B	IPR011650	Peptidase M20, dimerisation domain	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.