6X3M

Crystal structure of full-length Streptococcal bacteriophage hyaluronidase in complex with unsaturated hyaluronan octa-saccharides

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
D	SCOP2B Superfamily	Phage fibre proteins	8103376	3000351	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Phage fibre proteins	8103376	3000351	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Phage fibre proteins	8103376	3000351	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Phage fibre proteins	8103376	3000351	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Phage fibre proteins	8103376	3000351	SCOP2B (2022-06-29)
F	SCOP2 Family	HylP-like	8103375	4001933	SCOP2 (2022-06-29)
F	SCOP2 Superfamily	Phage fibre proteins	8103376	3000351	SCOP2 (2022-06-29)
G	SCOP2B Superfamily	Phage fibre proteins	8103376	3000351	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Phage fibre proteins	8103376	3000351	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	Phage fibre proteins	8103376	3000351	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)
D	Hyaluronidase_1	e6x3mD2	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: Hyaluronidase_1	ECOD (1.6)
D	EUF07876	e6x3mD1	A: beta duplicates or obligate multimers	X: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	H: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	T: Major tropism determinant (Mtd) trimerization domain-related	F: EUF07876	ECOD (1.6)
A	Hyaluronidase_1	e6x3mA2	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: Hyaluronidase_1	ECOD (1.6)
A	EUF07876	e6x3mA1	A: beta duplicates or obligate multimers	X: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	H: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	T: Major tropism determinant (Mtd) trimerization domain-related	F: EUF07876	ECOD (1.6)
B	Hyaluronidase_1	e6x3mB2	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: Hyaluronidase_1	ECOD (1.6)
B	EUF07876	e6x3mB1	A: beta duplicates or obligate multimers	X: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	H: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	T: Major tropism determinant (Mtd) trimerization domain-related	F: EUF07876	ECOD (1.6)
C	Hyaluronidase_1	e6x3mC1	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: Hyaluronidase_1	ECOD (1.6)
C	EUF07876	e6x3mC2	A: beta duplicates or obligate multimers	X: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	H: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	T: Major tropism determinant (Mtd) trimerization domain-related	F: EUF07876	ECOD (1.6)
E	Hyaluronidase_1	e6x3mE2	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: Hyaluronidase_1	ECOD (1.6)
E	EUF07876	e6x3mE1	A: beta duplicates or obligate multimers	X: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	H: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	T: Major tropism determinant (Mtd) trimerization domain-related	F: EUF07876	ECOD (1.6)
F	Hyaluronidase_1	e6x3mF2	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: Hyaluronidase_1	ECOD (1.6)
F	EUF07876	e6x3mF1	A: beta duplicates or obligate multimers	X: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	H: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	T: Major tropism determinant (Mtd) trimerization domain-related	F: EUF07876	ECOD (1.6)
G	Hyaluronidase_1	e6x3mG2	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: Hyaluronidase_1	ECOD (1.6)
G	EUF07876	e6x3mG1	A: beta duplicates or obligate multimers	X: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	H: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	T: Major tropism determinant (Mtd) trimerization domain-related	F: EUF07876	ECOD (1.6)
H	Hyaluronidase_1	e6x3mH2	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: Hyaluronidase_1	ECOD (1.6)
H	EUF07876	e6x3mH1	A: beta duplicates or obligate multimers	X: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	H: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	T: Major tropism determinant (Mtd) trimerization domain-related	F: EUF07876	ECOD (1.6)
I	Hyaluronidase_1	e6x3mI1	A: beta duplicates or obligate multimers	X: Phage tail fiber protein trimerization domain (From Topology)	H: Phage tail fiber protein trimerization domain (From Topology)	T: Phage tail fiber protein trimerization domain	F: Hyaluronidase_1	ECOD (1.6)
I	EUF07876	e6x3mI2	A: beta duplicates or obligate multimers	X: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	H: Major tropism determinant (Mtd) trimerization domain-related (From Topology)	T: Major tropism determinant (Mtd) trimerization domain-related	F: EUF07876	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H, I	PF18454	Major tropism determinant N-terminal domain (Mtd_N)	Major tropism determinant N-terminal domain	This is the N-terminal domain of major tropism determinant (Mtd), a retroelement-encoded receptor-binding protein. Mtd-N forms a three-fold symmetric beta-prism. This resembles the pseudo three-fold-symmetric beta-prisms of monocot lectins, but lacks ...	This is the N-terminal domain of major tropism determinant (Mtd), a retroelement-encoded receptor-binding protein. Mtd-N forms a three-fold symmetric beta-prism. This resembles the pseudo three-fold-symmetric beta-prisms of monocot lectins, but lacks residues in these lectins identified as binding carbohydrates. The beta-prism and beta-sandwich domains reinforce overall trimeric assembly and therefore may have indirect roles in stabilizing the backbone of the variable region [1].	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I	PF07212	Hyaluronidase protein (HylP) (Hyaluronidase_1)	Hyaluronidase protein (HylP)	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H, I	Hyaluronoglucosaminidase	hyalurononglucosaminidase activity hydrolase activity, acting on glycosyl bonds hexosaminidase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity	carbohydrate metabolic process polysaccharide biosynthetic process carbohydrate biosynthetic process primary metabolic process macromolecule biosynthetic process cellular component organization capsule organization polysaccharide metabolic process biosynthetic process metabolic process cellular process macromolecule metabolic process cellular component organization or biogenesis capsule polysaccharide biosynthetic process carbohydrate metabolic process polysaccharide biosynthetic process carbohydrate biosynthetic process primary metabolic process macromolecule biosynthetic process cellular component organization capsule organization polysaccharide metabolic process biosynthetic process metabolic process cellular process macromolecule metabolic process cellular component organization or biogenesis capsule polysaccharide biosynthetic process external encapsulating structure organization symbiont-mediated disruption of host anatomical structure biological process involved in interspecies interaction between organisms viral life cycle 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 envelope symbiont entry into host cell viral process symbiont entry into host disruption of anatomical structure in another organism symbiont entry into host cell via disruption of host cell glycocalyx	virion component

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR009860	Hyaluronidase, bacterial	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR041352	Major tropism determinant, N-terminal 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.