4LXC

The antimicrobial peptidase lysostaphin from Staphylococcus simulans

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	SH3_5	e4lxcA1	A: beta barrels	X: SH3	H: SH3	T: SH3	F: SH3_5	ECOD (1.6)
A	Peptidase_M23	e4lxcA2	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	SH3_5	e4lxcD1	A: beta barrels	X: SH3	H: SH3	T: SH3	F: SH3_5	ECOD (1.6)
D	Peptidase_M23	e4lxcD2	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	SH3_5	e4lxcB1	A: beta barrels	X: SH3	H: SH3	T: SH3	F: SH3_5	ECOD (1.6)
B	Peptidase_M23	e4lxcB2	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	SH3_5	e4lxcC1	A: beta barrels	X: SH3	H: SH3	T: SH3	F: SH3_5	ECOD (1.6)
C	Peptidase_M23	e4lxcC2	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	2.70.70.10	Mainly Beta	Distorted Sandwich	Glucose Permease (Domain IIA)	Glucose Permease (Domain IIA)	CATH (4.3.0)
A	2.30.30.40	Mainly Beta	Roll	SH3 type barrels.	SH3 Domains	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)
D	2.30.30.40	Mainly Beta	Roll	SH3 type barrels.	SH3 Domains	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)
B	2.30.30.40	Mainly Beta	Roll	SH3 type barrels.	SH3 Domains	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)
C	2.30.30.40	Mainly Beta	Roll	SH3 type barrels.	SH3 Domains	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF08460	Bacterial SH3 domain (SH3_5)	Bacterial SH3 domain	-	Domain
A, B, C, D	PF01551	Peptidase family M23 (Peptidase_M23)	Peptidase family M23	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Lysostaphin	cation binding ion binding binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein metalloendopeptidase activity hydrolase activity metallopeptidase activity catalytic activity endopeptidase activity	proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process cellular component organization cell wall organization or biogenesis cell wall organization cellular component organization or biogenesis external encapsulating structure organization	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR050570	Bacterial cell wall metabolism enzyme	Family
A, B, C, D	IPR003646	SH3-like domain, bacterial-type	Domain
A, B, C, D	IPR016047	Peptidase M23	Domain
A, B, C, D	IPR046567	Lysostaphin, N-terminal domain	Domain
A, B, C, D	IPR011055	Duplicated hybrid motif	Homologous Superfamily

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.