3CSQ | pdb_00003csq

Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
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	LT_GEWL_like	e3csqA6	A: a+b complex topology	X: Lysozyme-like (From Homology)	H: Lysozyme-like	T: Lysozyme-like	F: LT_GEWL_like	ECOD (1.6)
A	Peptidase_M23	e3csqA5	A: a+b complex topology	X: alpha/beta-Hammerhead/Barrel-sandwich hybrid	H: alpha/beta-Hammerhead/Barrel-sandwich hybrid	T: Duplicated hybrid motif	F: Peptidase_M23	ECOD (1.6)
B	LT_GEWL_like	e3csqB6	A: a+b complex topology	X: Lysozyme-like (From Homology)	H: Lysozyme-like	T: Lysozyme-like	F: LT_GEWL_like	ECOD (1.6)
B	Peptidase_M23	e3csqB5	A: a+b complex topology	X: alpha/beta-Hammerhead/Barrel-sandwich hybrid	H: alpha/beta-Hammerhead/Barrel-sandwich hybrid	T: Duplicated hybrid motif	F: Peptidase_M23	ECOD (1.6)
C	LT_GEWL_like	e3csqC6	A: a+b complex topology	X: Lysozyme-like (From Homology)	H: Lysozyme-like	T: Lysozyme-like	F: LT_GEWL_like	ECOD (1.6)
C	Peptidase_M23	e3csqC5	A: a+b complex topology	X: alpha/beta-Hammerhead/Barrel-sandwich hybrid	H: alpha/beta-Hammerhead/Barrel-sandwich hybrid	T: Duplicated hybrid motif	F: Peptidase_M23	ECOD (1.6)
D	LT_GEWL_like	e3csqD6	A: a+b complex topology	X: Lysozyme-like (From Homology)	H: Lysozyme-like	T: Lysozyme-like	F: LT_GEWL_like	ECOD (1.6)
D	Peptidase_M23	e3csqD5	A: a+b complex topology	X: alpha/beta-Hammerhead/Barrel-sandwich hybrid	H: alpha/beta-Hammerhead/Barrel-sandwich hybrid	T: Duplicated hybrid motif	F: Peptidase_M23	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.530.10	Mainly Alpha	Orthogonal Bundle	Lysozyme		CATH (4.3.0)
A	2.70.70.10	Mainly Beta	Distorted Sandwich	Glucose Permease (Domain IIA)	Glucose Permease (Domain IIA)	CATH (4.3.0)
B	1.10.530.10	Mainly Alpha	Orthogonal Bundle	Lysozyme		CATH (4.3.0)
B	2.70.70.10	Mainly Beta	Distorted Sandwich	Glucose Permease (Domain IIA)	Glucose Permease (Domain IIA)	CATH (4.3.0)
C	1.10.530.10	Mainly Alpha	Orthogonal Bundle	Lysozyme		CATH (4.3.0)
C	2.70.70.10	Mainly Beta	Distorted Sandwich	Glucose Permease (Domain IIA)	Glucose Permease (Domain IIA)	CATH (4.3.0)
D	1.10.530.10	Mainly Alpha	Orthogonal Bundle	Lysozyme		CATH (4.3.0)
D	2.70.70.10	Mainly Beta	Distorted Sandwich	Glucose Permease (Domain IIA)	Glucose Permease (Domain IIA)	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF18013	Phage tail lysozyme (Phage_lysozyme2)	Phage tail lysozyme	This domain has a lysozyme like fold. It is found in the tail protein of various phages probably giving them the ability to degrade the host cell wall peptidoglycan layer [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Morphogenesis protein 1	peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity hydrolase activity, acting on glycosyl bonds cation binding ion binding binding metal ion binding small molecule binding	virion assembly viral tail assembly virus tail fiber assembly viral process viral life cycle symbiont-mediated disruption of host anatomical structure biological process involved in interspecies interaction between organisms disruption of cell wall in another organism symbiont-mediated disruption of host cell wall symbiont-mediated disruption of host cell envelope symbiont-mediated disruption of host cellular anatomical structure biological process involved in interaction with host biological process involved in symbiotic interaction symbiont entry into host cell via disruption of host cell wall peptidoglycan virion assembly viral tail assembly virus tail fiber assembly viral process viral life cycle symbiont-mediated disruption of host anatomical structure biological process involved in interspecies interaction between organisms disruption of cell wall in another organism symbiont-mediated disruption of host cell wall symbiont-mediated disruption of host cell envelope symbiont-mediated disruption of host cellular anatomical structure biological process involved in interaction with host biological process involved in symbiotic interaction symbiont entry into host cell via disruption of host cell wall peptidoglycan disruption of cellular anatomical structure in another organism symbiont entry into host cell symbiont entry into host disruption of anatomical structure in another organism symbiont genome ejection through host cell envelope symbiont genome ejection through host cell envelope, short tail mechanism cellular component organization cell wall organization or biogenesis cell wall organization cellular process cellular component organization or biogenesis external encapsulating structure organization symbiont entry into host cell via disruption of host cell envelope disruption of cell in another organism killing of cells of another organism cell killing proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process response to stimulus response to other organism defense response response to external stimulus response to biotic stimulus defense response to bacterium defense response to other organism response to stress response to bacterium response to external biotic stimulus	virus tail virion component virus tail, tip

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR011055	Duplicated hybrid motif	Homologous Superfamily
A, B, C, D	IPR041219	Phage tail lysozyme	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.