3GPQ

Crystal structure of macro domain of Chikungunya virus in complex with RNA

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
D	SCOP2 Family	Macro domain	8063767	4000521	SCOP2 (2022-06-29)
D	SCOP2 Superfamily	Macro domain-like	8063768	3000458	SCOP2 (2022-06-29)
A	SCOP2B Superfamily	Macro domain-like	8063768	3000458	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Macro domain-like	8063768	3000458	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Macro domain-like	8063768	3000458	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	Macro_3	e3gpqD1	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: Macro_3	ECOD (1.6)
A	Macro_3	e3gpqA1	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: Macro_3	ECOD (1.6)
B	Macro_3	e3gpqB1	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: Macro_3	ECOD (1.6)
C	Macro_3	e3gpqC1	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: Macro_3	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
D	3.40.220.10	Alpha Beta	3-Layer(aba) Sandwich	Leucine Aminopeptidase, subunit E	domain 1	CATH (4.3.0)
A	3.40.220.10	Alpha Beta	3-Layer(aba) Sandwich	Leucine Aminopeptidase, subunit E	domain 1	CATH (4.3.0)
B	3.40.220.10	Alpha Beta	3-Layer(aba) Sandwich	Leucine Aminopeptidase, subunit E	domain 1	CATH (4.3.0)
C	3.40.220.10	Alpha Beta	3-Layer(aba) Sandwich	Leucine Aminopeptidase, subunit E	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF01661	Macro domain (Macro)	Macro domain	The Macro or A1pp domain is a module of about 180 amino acids which can bind ADP-ribose (an NAD metabolite) or related ligands. Binding to ADP-ribose could be either covalent or non-covalent [1]: in certain cases it is believed to bind non-covalently ...	The Macro or A1pp domain is a module of about 180 amino acids which can bind ADP-ribose (an NAD metabolite) or related ligands. Binding to ADP-ribose could be either covalent or non-covalent [1]: in certain cases it is believed to bind non-covalently [2]; while in other cases (such as Aprataxin) it appears to bind both non-covalently through a zinc finger motif, and covalently through a separate region of the protein [3]. This domain is found in a number of otherwise unrelated proteins. It is found at the C-terminus of the macro-H2A histone protein 4 and also in the non-structural proteins of several types of ssRNA viruses such as NSP3 from alpha-viruses and coronaviruses. This domain is also found on its own in a family of proteins from bacteria, archaebacteria and eukaryotes. The 3D structure of the SARS-CoV Macro domain has a mixed alpha/beta fold consisting of a central seven-stranded twisted mixed beta sheet sandwiched between two alpha helices on one face, and three on the other. The final alpha-helix, located on the edge of the central beta-sheet, forms the C terminus of the protein [4]. The crystal structure of AF1521 (a Macro domain-only protein from Archaeoglobus fulgidus) has also been reported and compared with other Macro domain containing proteins. Several Macro domain only proteins are shorter than AF1521, and appear to lack either the first strand of the beta-sheet or the C-terminal helix 5. Well conserved residues form a hydrophobic cleft and cluster around the AF1521-ADP-ribose binding site [5].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Non-structural protein 3	5'-3' RNA polymerase activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid RNA polymerase activity transferase activity RNA-dependent RNA polymerase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups RNA methyltransferase activity transferase activity, transferring one-carbon groups methyltransferase activity S-adenosylmethionine-dependent methyltransferase activity mRNA methyltransferase activity 5'-3' RNA polymerase activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid RNA polymerase activity transferase activity RNA-dependent RNA polymerase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups RNA methyltransferase activity transferase activity, transferring one-carbon groups methyltransferase activity S-adenosylmethionine-dependent methyltransferase activity mRNA methyltransferase activity cysteine-type peptidase activity peptidase activity catalytic activity, acting on a protein hydrolase activity RNA binding binding organic cyclic compound binding nucleic acid binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding pyrophosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity, acting on acid anhydrides mRNA 5'-triphosphate monophosphatase activity adenyl ribonucleotide binding adenyl nucleotide binding ATP binding phosphoric ester hydrolase activity hydrolase activity, acting on ester bonds polynucleotide 5'-phosphatase activity phosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity ATP-dependent activity poly(A) RNA polymerase activity adenylyltransferase activity helicase activity RNA helicase activity ATP-dependent activity, acting on RNA cation binding metal ion binding	symbiont-mediated suppression of host transcription biological process involved in interspecies interaction between organisms symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity symbiont-mediated perturbation of host process modulation of process of another organism biological process involved in interaction with host biological process involved in symbiotic interaction RNA metabolic process viral life cycle primary metabolic process nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process RNA biosynthetic process symbiont-mediated suppression of host transcription biological process involved in interspecies interaction between organisms symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity symbiont-mediated perturbation of host process modulation of process of another organism biological process involved in interaction with host biological process involved in symbiotic interaction RNA metabolic process viral life cycle primary metabolic process nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process nucleic acid biosynthetic process viral genome replication biosynthetic process viral RNA genome replication viral process metabolic process cellular process macromolecule metabolic process mRNA modification mRNA metabolic process RNA modification macromolecule modification symbiont-mediated perturbation of host cellular process symbiont-mediated suppression of host JAK-STAT cascade symbiont-mediated suppression of host signal transduction pathway symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT activity symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity symbiont-mediated perturbation of host signal transduction pathway methylation regulation of cytoskeleton organization regulation of biological process regulation of cellular component organization regulation of cellular process biological regulation regulation of organelle organization cellular component organization organelle organization cellular component organization or biogenesis cytoskeleton organization gene expression DNA-templated transcription symbiont-mediated perturbation of host defense response modulation by virus of host process virus-mediated perturbation of host defense response modulation by virus of host cellular process 7-methylguanosine mRNA capping 7-methylguanosine RNA capping RNA capping mRNA processing RNA 5'-end processing RNA processing proteolysis protein metabolic process response to host defenses response to stimulus response to other organism symbiont-mediated perturbation of host immune response symbiont-mediated perturbation of host defenses response to defenses of other organism response to external stimulus response to biotic stimulus symbiont-mediated suppression of host immune response symbiont-mediated suppression of host innate immune response symbiont-mediated suppression of host defenses symbiont-mediated perturbation of host innate immune response response to host response to external biotic stimulus symbiont-mediated suppression of host interferon-mediated signaling pathway symbiont-mediated suppression of host type I interferon-mediated signaling pathway	cellular anatomical structure membrane host cell plasma membrane host cellular component host cell part host cell membrane host intracellular membrane-bounded organelle host intracellular part host cell cytoplasmic vesicle membrane host cell cytoplasm part host intracellular organelle host cell cytoplasmic vesicle host cell cytoplasm host intracellular region cellular anatomical structure membrane host cell plasma membrane host cellular component host cell part host cell membrane host intracellular membrane-bounded organelle host intracellular part host cell cytoplasmic vesicle membrane host cell cytoplasm part host intracellular organelle host cell cytoplasmic vesicle host cell cytoplasm host intracellular region host cell filopodium host cell projection host cell nucleus
E, F	RNA (5'-R(APAP*A)-3')	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR047311	RNA-dependent RNA polymerase, togavirus	Domain
A, B, C, D	IPR048891	Non-structural protein 3, zinc-binding domain	Domain
A, B, C, D	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
A, B, C, D	IPR002589	Macro domain	Domain
A, B, C, D	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily	Homologous Superfamily
A, B, C, D	IPR002620	Alphavirus nsp2 protease domain	Domain
A, B, C, D	IPR043502	DNA/RNA polymerase superfamily	Homologous Superfamily
A, B, C, D	IPR001788	RNA-dependent RNA polymerase, alsuviricetes	Domain
A, B, C, D	IPR002588	Alphavirus-like methyltransferase domain	Domain
A, B, C, D	IPR043472	Macro domain-like	Homologous Superfamily
A, B, C, D	IPR044936	Alphavirus nsP2 protease domain superfamily	Homologous Superfamily
A, B, C, D	IPR049329	Tomato mosaic virus helicase, N-terminal domain	Domain
A, B, C, D	IPR044371	Non-structural protein 3, X-domain-like	Domain
A, B, C, D	IPR027351	(+) RNA virus helicase core domain	Domain
A, B, C, D	IPR007094	RNA-directed RNA polymerase, catalytic 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.