5HXF

Crystal structure of 3C protease from a mild Human enterovirus 71 in complex with rupintrivir

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5hxfa1	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	automated matches	automated matches	EV71 (Enterovirus A71 ) [TaxId: 39054 ],	SCOPe (2.08)
A	d5hxfa2	Artifacts	Tags	Tags	Tags	N-terminal Tags	EV71 (Enterovirus A71 ) [TaxId: 39054 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Viral cysteine protease of trypsin fold, (3C/2A)Pro-like	8071514	4007776	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Trypsin-like serine proteases	8071515	3000114	SCOP2 (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	Peptidase_C3	e5hxfA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: Peptidase_C3	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00548	3C cysteine protease (picornain 3C) (Peptidase_C3)	3C cysteine protease (picornain 3C)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	3C protease	cysteine-type peptidase activity peptidase activity catalytic activity, acting on a protein cysteine-type endopeptidase activity hydrolase activity catalytic activity endopeptidase activity	virion attachment to host cell biological process involved in interspecies interaction between organisms adhesion of symbiont to host cell viral process viral life cycle adhesion of symbiont to host biological process involved in interaction with host biological process involved in symbiotic interaction proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process virion attachment to host cell biological process involved in interspecies interaction between organisms adhesion of symbiont to host cell viral process viral life cycle adhesion of symbiont to host biological process involved in interaction with host biological process involved in symbiotic interaction proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process symbiont entry into host cell symbiont entry into host	cellular anatomical structure intracellular anatomical structure cytoplasm host cellular component host intracellular part host cell cytoplasm host cell part host intracellular region viral capsid icosahedral viral capsid virion component T=pseudo3 icosahedral viral capsid

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
A	IPR044067	Picornavirales 3C/3C-like protease domain	Domain
A	IPR000199	Peptidase C3A/C3B, picornaviral	Domain
A	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	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.