6S4S

CBDP35 Native structure

External Resource: Annotation

Domain Annotation: ECOD Classification
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)
A	PF18341	e6s4sA2	A: beta barrels	X: SH3	H: SH3	T: SH3	F: PF18341	ECOD (1.6)
B	PF18341	e6s4sB2	A: beta barrels	X: SH3	H: SH3	T: SH3	F: PF18341	ECOD (1.6)
D	PF18341	e6s4sD2	A: beta barrels	X: SH3	H: SH3	T: SH3	F: PF18341	ECOD (1.6)
E	PF18341	e6s4sE2	A: beta barrels	X: SH3	H: SH3	T: SH3	F: PF18341	ECOD (1.6)
F	PF18341	e6s4sF2	A: beta barrels	X: SH3	H: SH3	T: SH3	F: PF18341	ECOD (1.6)
G	PF18341	e6s4sG2	A: beta barrels	X: SH3	H: SH3	T: SH3	F: PF18341	ECOD (1.6)
H	PF18341	e6s4sH2	A: beta barrels	X: SH3	H: SH3	T: SH3	F: PF18341	ECOD (1.6)
I	PF18341	e6s4sI2	A: beta barrels	X: SH3	H: SH3	T: SH3	F: PF18341	ECOD (1.6)
K [auth L]	PF18341	e6s4sL2	A: beta barrels	X: SH3	H: SH3	T: SH3	F: PF18341	ECOD (1.6)
L [auth K]	PF18341	e6s4sK2	A: beta barrels	X: SH3	H: SH3	T: SH3	F: PF18341	ECOD (1.6)
C	PF18341	e6s4sC2	A: beta barrels	X: SH3	H: SH3	T: SH3	F: PF18341	ECOD (1.6)
J	PF18341	e6s4sJ2	A: beta barrels	X: SH3	H: SH3	T: SH3	F: PF18341	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF18341	PSA endolysin C-terminal cell wall binding domain (PSA_CBD)	PSA endolysin C-terminal cell wall binding domain	This is the C-terminal domain of bacteriophage PSA endolysin. The C-terminal domain is the cell wall-binding domain (CBD) which is composed of two structurally homologous subdomains. CBD comprises two copies of a beta-barrel-like folds, which are hel ...	This is the C-terminal domain of bacteriophage PSA endolysin. The C-terminal domain is the cell wall-binding domain (CBD) which is composed of two structurally homologous subdomains. CBD comprises two copies of a beta-barrel-like folds, which are held together by means of swapped beta-strands. The observed structure of the CBD sub-domains from Listeriaphage endolysin (N-acetyl-muramoyl-l-alanine amidase), could be the result of either a gene duplication during evolution of the CBD or the pick-up of another functionally equivalent coding sequence, followed by swapping of the respective ancestral leading beta-strands [1].	Domain
B, D, E, F, G, B, D, E, F, G, H, I, K [auth L], L [auth K]	PF18341	PSA endolysin C-terminal cell wall binding domain (PSA_CBD)	PSA endolysin C-terminal cell wall binding domain	This is the C-terminal domain of bacteriophage PSA endolysin. The C-terminal domain is the cell wall-binding domain (CBD) which is composed of two structurally homologous subdomains. CBD comprises two copies of a beta-barrel-like folds, which are hel ...	This is the C-terminal domain of bacteriophage PSA endolysin. The C-terminal domain is the cell wall-binding domain (CBD) which is composed of two structurally homologous subdomains. CBD comprises two copies of a beta-barrel-like folds, which are held together by means of swapped beta-strands. The observed structure of the CBD sub-domains from Listeriaphage endolysin (N-acetyl-muramoyl-l-alanine amidase), could be the result of either a gene duplication during evolution of the CBD or the pick-up of another functionally equivalent coding sequence, followed by swapping of the respective ancestral leading beta-strands [1].	Domain
C, J	PF18341	PSA endolysin C-terminal cell wall binding domain (PSA_CBD)	PSA endolysin C-terminal cell wall binding domain	This is the C-terminal domain of bacteriophage PSA endolysin. The C-terminal domain is the cell wall-binding domain (CBD) which is composed of two structurally homologous subdomains. CBD comprises two copies of a beta-barrel-like folds, which are hel ...	This is the C-terminal domain of bacteriophage PSA endolysin. The C-terminal domain is the cell wall-binding domain (CBD) which is composed of two structurally homologous subdomains. CBD comprises two copies of a beta-barrel-like folds, which are held together by means of swapped beta-strands. The observed structure of the CBD sub-domains from Listeriaphage endolysin (N-acetyl-muramoyl-l-alanine amidase), could be the result of either a gene duplication during evolution of the CBD or the pick-up of another functionally equivalent coding sequence, followed by swapping of the respective ancestral leading beta-strands [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PlyP35	peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity	-	-
B, D, E, F, G, B, D, E, F, G, H, I, K [auth L], L [auth K]	PlyP35	peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity	-	-
C, J	PlyP35	peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR009045	Hedgehog signalling/DD-peptidase zinc-binding domain superfamily	Homologous Superfamily
A	IPR039561	Peptidase M15C	Domain
A	IPR041341	PSA endolysin, cell wall binding domain	Domain
B, D, E, F, G, B, D, E, F, G, H, I, K [auth L], L [auth K]	IPR009045	Hedgehog signalling/DD-peptidase zinc-binding domain superfamily	Homologous Superfamily
B, D, E, F, G, B, D, E, F, G, H, I, K [auth L], L [auth K]	IPR039561	Peptidase M15C	Domain
B, D, E, F, G, B, D, E, F, G, H, I, K [auth L], L [auth K]	IPR041341	PSA endolysin, cell wall binding domain	Domain
C, J	IPR009045	Hedgehog signalling/DD-peptidase zinc-binding domain superfamily	Homologous Superfamily
C, J	IPR039561	Peptidase M15C	Domain
C, J	IPR041341	PSA endolysin, cell wall binding 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 R01GM133198.