2VO9

CRYSTAL STRUCTURE OF THE ENZYMATICALLY ACTIVE DOMAIN OF THE LISTERIA MONOCYTOGENES BACTERIOPHAGE 500 ENDOLYSIN PLY500

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 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	d2vo9a1	Alpha and beta proteins (a+b)	Hedgehog/DD-peptidase	Hedgehog/DD-peptidase	VanY-like	L-alanyl-D-glutamate peptidase Ply	(Listeria phage A500 ) [TaxId: 40522 ],	SCOPe (2.08)
A	d2vo9a2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Listeria phage A500 ) [TaxId: 40522 ],	SCOPe (2.08)
B	d2vo9b2	Alpha and beta proteins (a+b)	Hedgehog/DD-peptidase	Hedgehog/DD-peptidase	VanY-like	automated matches	(Listeria phage A500 ) [TaxId: 40522 ],	SCOPe (2.08)
B	d2vo9b3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Listeria phage A500 ) [TaxId: 40522 ],	SCOPe (2.08)
C	d2vo9c2	Alpha and beta proteins (a+b)	Hedgehog/DD-peptidase	Hedgehog/DD-peptidase	VanY-like	automated matches	(Listeria phage A500 ) [TaxId: 40522 ],	SCOPe (2.08)
C	d2vo9c3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Listeria phage A500 ) [TaxId: 40522 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	VanY-like	8025249	4002064	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Hedgehog/DD-peptidase	8037628	3001458	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Hedgehog/DD-peptidase	8037628	3001458	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Hedgehog/DD-peptidase	8037628	3001458	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	PF13539	e2vo9A1	A: a+b two layers	X: Hedgehog/DD-peptidase (From Topology)	H: Hedgehog/DD-peptidase (From Topology)	T: Hedgehog/DD-peptidase	F: PF13539	ECOD (1.6)
B	PF13539	e2vo9B1	A: a+b two layers	X: Hedgehog/DD-peptidase (From Topology)	H: Hedgehog/DD-peptidase (From Topology)	T: Hedgehog/DD-peptidase	F: PF13539	ECOD (1.6)
C	PF13539	e2vo9C1	A: a+b two layers	X: Hedgehog/DD-peptidase (From Topology)	H: Hedgehog/DD-peptidase (From Topology)	T: Hedgehog/DD-peptidase	F: PF13539	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.1380.10	Alpha Beta	2-Layer Sandwich	Muramoyl-pentapeptide Carboxypeptidase	domain 2	CATH (4.3.0)
B	3.30.1380.10	Alpha Beta	2-Layer Sandwich	Muramoyl-pentapeptide Carboxypeptidase	domain 2	CATH (4.3.0)
C	3.30.1380.10	Alpha Beta	2-Layer Sandwich	Muramoyl-pentapeptide Carboxypeptidase	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF13539	D-alanyl-D-alanine carboxypeptidase (Peptidase_M15_4)	D-alanyl-D-alanine carboxypeptidase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	L-ALANYL-D-GLUTAMATE PEPTIDASE	peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity	cellular component organization cell wall organization or biogenesis cell wall organization cellular process cellular component organization or biogenesis external encapsulating structure organization	extracellular region cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR009045	Hedgehog signalling/DD-peptidase zinc-binding domain superfamily	Homologous Superfamily
A, B, C	IPR039561	Peptidase M15C	Domain
A, B, C	IPR041341	PSA endolysin, cell wall binding domain	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.