3EV6

Crystal Structure of Ribonuclease A in 50% R,S,R-Bisfuranol

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)
B	d3ev6b_	Alpha and beta proteins (a+b)	RNase A-like	RNase A-like	Ribonuclease A-like	automated matches	(Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
A	d3ev6a_	Alpha and beta proteins (a+b)	RNase A-like	RNase A-like	Ribonuclease A-like	automated matches	(Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	RNase A-like	8038165	3001918	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	RNase A-like	8038165	3001918	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)
B	RnaseA	e3ev6B1	A: a+b complex topology	X: RNase A-like	H: RNase A-like (From Topology)	T: RNase A-like	F: RnaseA	ECOD (1.6)
A	RnaseA	e3ev6A1	A: a+b complex topology	X: RNase A-like	H: RNase A-like (From Topology)	T: RNase A-like	F: RnaseA	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.10.130.10	Alpha Beta	Roll	P-30 Protein	Ribonuclease A-like domain	CATH (4.3.0)
A	3.10.130.10	Alpha Beta	Roll	P-30 Protein	Ribonuclease A-like domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00074	Pancreatic ribonuclease (RnaseA)	Pancreatic ribonuclease	Ribonucleases. Members include pancreatic RNAase A and angiogenins. Structure is an alpha+beta fold -- long curved beta sheet and three helices.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Ribonuclease pancreatic	endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters endonuclease activity ribonuclease A activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid RNA nuclease activity hydrolase activity RNA endonuclease activity, producing 3'-phosphomonoesters nuclease activity hydrolase activity, acting on ester bonds RNA endonuclease activity catalytic activity lyase activity binding endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters endonuclease activity ribonuclease A activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid RNA nuclease activity hydrolase activity RNA endonuclease activity, producing 3'-phosphomonoesters nuclease activity hydrolase activity, acting on ester bonds RNA endonuclease activity catalytic activity lyase activity binding organic cyclic compound binding nucleic acid binding	biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response defense response to Gram-positive bacterium 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	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR023412	Ribonuclease A-domain	Domain
A, B	IPR036816	Ribonuclease A-like domain superfamily	Homologous Superfamily
A, B	IPR001427	Pancreatic ribonuclease	Family
A, B	IPR023411	Ribonuclease A, active site	Active Site

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.