Annotations: 3VDX

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Influenza virus matrix protein M1-like	8038312	3000900	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	alpha/beta-Hydrolases	8032554	3000102	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	alpha/beta-Hydrolases	8032554	3000102	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Influenza virus matrix protein M1-like	8038312	3000900	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	alpha/beta-Hydrolases	8032554	3000102	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Influenza virus matrix protein M1-like	8038312	3000900	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	PF00598	e3vdxA2	A: alpha complex topology	X: Influenza virus matrix protein M1 (From Topology)	H: Influenza virus matrix protein M1 (From Topology)	T: Influenza virus matrix protein M1	F: PF00598	ECOD (1.6)
A	PF00561	e3vdxA1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF00561	ECOD (1.6)
B	PF00598	e3vdxB1	A: alpha complex topology	X: Influenza virus matrix protein M1 (From Topology)	H: Influenza virus matrix protein M1 (From Topology)	T: Influenza virus matrix protein M1	F: PF00598	ECOD (1.6)
B	PF00561	e3vdxB2	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF00561	ECOD (1.6)
C	PF00598	e3vdxC1	A: alpha complex topology	X: Influenza virus matrix protein M1 (From Topology)	H: Influenza virus matrix protein M1 (From Topology)	T: Influenza virus matrix protein M1	F: PF00598	ECOD (1.6)
C	PF00561	e3vdxC2	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF00561	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
A	1.20.91.10	Mainly Alpha	Up-down Bundle	Influenza Virus Matrix Protein	Chain A, domain 1	CATH (4.3.0)
A	1.10.10.180	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Influenza matrix protein M1, N-terminal subdomain 2	CATH (4.3.0)
B	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
B	1.20.91.10	Mainly Alpha	Up-down Bundle	Influenza Virus Matrix Protein	Chain A, domain 1	CATH (4.3.0)
B	1.10.10.180	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Influenza matrix protein M1, N-terminal subdomain 2	CATH (4.3.0)
C	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
C	1.20.91.10	Mainly Alpha	Up-down Bundle	Influenza Virus Matrix Protein	Chain A, domain 1	CATH (4.3.0)
C	1.10.10.180	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Influenza matrix protein M1, N-terminal subdomain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF00561	alpha/beta hydrolase fold (Abhydrolase_1)	alpha/beta hydrolase fold	This catalytic domain is found in a very wide range of enzymes.	Domain
A, B, C	PF00598	Influenza Matrix protein (M1) (Flu_M1)	Influenza Matrix protein (M1)	This protein forms a continuous shell on the inner side of the lipid bilayer, but its function is unclear.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Designed 16nm tetrahedral protein cage containing Non-haem bromoperoxidase BPO-A2 and Matrix protein 1	peroxidase activity oxidoreductase activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor catalytic activity structural constituent of virion structural molecule activity RNA binding binding organic cyclic compound binding nucleic acid binding	antibiotic metabolic process biosynthetic process metabolic process antibiotic biosynthetic process biological process involved in interspecies interaction between organisms non-lytic viral release viral budding viral life cycle biological process involved in interaction with host biological process involved in symbiotic interaction virion assembly exit from host cell viral process viral budding from plasma membrane antibiotic metabolic process biosynthetic process metabolic process antibiotic biosynthetic process biological process involved in interspecies interaction between organisms non-lytic viral release viral budding viral life cycle biological process involved in interaction with host biological process involved in symbiotic interaction virion assembly exit from host cell viral process viral budding from plasma membrane viral release from host cell	virion component virion membrane extracellular region cellular anatomical entity cell periphery plasma membrane membrane host intracellular membrane-bounded organelle host cellular component host intracellular part host cell part host intracellular region host cell nucleus host intracellular organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR000639	Epoxide hydrolase-like	Family
A, B, C	IPR000073	Alpha/beta hydrolase fold-1	Domain
A, B, C	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily
A, B, C	IPR015799	Influenza matrix M1, N-terminal subdomain 2	Homologous Superfamily
A, B, C	IPR015423	Influenza matrix M1, N-terminal subdomain 1	Homologous Superfamily
A, B, C	IPR036039	Influenza virus matrix protein M1	Homologous Superfamily
A, B, C	IPR013188	Influenza matrix M1, C-terminal	Domain
A, B, C	IPR001561	Influenza matrix M1, N-terminal	Domain
A, B, C	IPR037533	Matrix protein 1	Family

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.