+Open data
-Basic information
Entry | Database: PDB / ID: 2n5l | ||||||
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Title | Regnase-1 C-terminal domain | ||||||
Components | Ribonuclease ZC3H12A | ||||||
Keywords | HYDROLASE / Regnase / Regnase-1 / Zc3h12a | ||||||
Function / homology | Function and homology information immune response-activating signaling pathway / positive regulation of miRNA catabolic process / positive regulation of protein deubiquitination / cellular response to ionomycin / miRNA catabolic process / RNA exonuclease activity / positive regulation of mRNA catabolic process / rough endoplasmic reticulum membrane / negative regulation by host of viral genome replication / cellular response to sodium arsenite ...immune response-activating signaling pathway / positive regulation of miRNA catabolic process / positive regulation of protein deubiquitination / cellular response to ionomycin / miRNA catabolic process / RNA exonuclease activity / positive regulation of mRNA catabolic process / rough endoplasmic reticulum membrane / negative regulation by host of viral genome replication / cellular response to sodium arsenite / negative regulation of T-helper 17 cell differentiation / negative regulation of muscle cell apoptotic process / nuclease activity / 3'-UTR-mediated mRNA destabilization / positive regulation of lipid storage / negative regulation of cardiac muscle contraction / negative regulation of nitric oxide biosynthetic process / mRNA 3'-UTR AU-rich region binding / cellular response to chemokine / negative regulation of non-canonical NF-kappaB signal transduction / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / miRNA binding / negative regulation of interleukin-1 beta production / positive regulation of p38MAPK cascade / negative regulation of NF-kappaB transcription factor activity / protein deubiquitination / positive regulation of execution phase of apoptosis / mRNA catabolic process / negative regulation of interleukin-6 production / negative regulation of type II interferon production / negative regulation of tumor necrosis factor production / negative regulation of cytokine production involved in inflammatory response / positive regulation of fat cell differentiation / cellular response to interleukin-1 / cellular response to glucose starvation / positive regulation of autophagy / negative regulation of canonical NF-kappaB signal transduction / rough endoplasmic reticulum / positive regulation of defense response to virus by host / RNA endonuclease activity / positive regulation of endothelial cell migration / negative regulation of protein phosphorylation / mRNA 3'-UTR binding / P-body / cellular response to virus / cytoplasmic ribonucleoprotein granule / positive regulation of protein import into nucleus / RNA stem-loop binding / positive regulation of angiogenesis / positive regulation of reactive oxygen species metabolic process / ribosome binding / protein complex oligomerization / cellular response to tumor necrosis factor / nervous system development / T cell receptor signaling pathway / cellular response to oxidative stress / cellular response to lipopolysaccharide / angiogenesis / cysteine-type deubiquitinase activity / Hydrolases; Acting on ester bonds / cell differentiation / cytoskeleton / inflammatory response / negative regulation of gene expression / mRNA binding / apoptotic process / DNA damage response / chromatin binding / positive regulation of gene expression / positive regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / nucleoplasm / nucleus / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / distance geometry | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Yokogawa, M. / Tsushima, T. / Noda, N.N. / Kumeta, H. / Adachi, W. / Enokizono, Y. / Yamashita, K. / Standley, D.M. / Takeuchi, O. / Akira, S. / Inagaki, F. | ||||||
Citation | Journal: Sci Rep / Year: 2016 Title: Structural basis for the regulation of enzymatic activity of Regnase-1 by domain-domain interactions Authors: Yokogawa, M. / Tsushima, T. / Noda, N.N. / Kumeta, H. / Enokizono, Y. / Yamashita, K. / Standley, D.M. / Takeuchi, O. / Akira, S. / Inagaki, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2n5l.cif.gz | 404 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2n5l.ent.gz | 343 KB | Display | PDB format |
PDBx/mmJSON format | 2n5l.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2n5l_validation.pdf.gz | 436.1 KB | Display | wwPDB validaton report |
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Full document | 2n5l_full_validation.pdf.gz | 553.1 KB | Display | |
Data in XML | 2n5l_validation.xml.gz | 21.1 KB | Display | |
Data in CIF | 2n5l_validation.cif.gz | 33.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n5/2n5l ftp://data.pdbj.org/pub/pdb/validation_reports/n5/2n5l | HTTPS FTP |
-Related structure data
Related structure data | 2n5jC 2n5kC 5h9vC 5h9wC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 6383.400 Da / Num. of mol.: 1 / Fragment: UNP residues 544-596 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Zc3h12a / Production host: Escherichia coli (E. coli) References: UniProt: Q5D1E7, Hydrolases; Acting on ester bonds |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 2.3 mM [U-99% 13C; U-99% 15N] Reg1_CTD-1, 10% v/v DSS-2, 0.02 mL [U-2H] D2O-3, 20 mM HEPES-4, 150 mM sodium chloride-5, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 170 / pH: 6.8 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Agilent INOVA / Manufacturer: Agilent / Model: INOVA / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: distance geometry / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |