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- PDB-8im5: Solution structure of the mouse HOIL1-L NZF domain in the free form -
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Open data
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Basic information
Entry | Database: PDB / ID: 8im5 | ||||||||||||
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Title | Solution structure of the mouse HOIL1-L NZF domain in the free form | ||||||||||||
![]() | RanBP-type and C3HC4-type zinc finger-containing protein 1 | ||||||||||||
![]() | IMMUNE SYSTEM / Ubiquitin-binding | ||||||||||||
Function / homology | ![]() TNFR1-induced proapoptotic signaling / TNFR1-induced NF-kappa-B signaling pathway / protein linear polyubiquitination / Regulation of TNFR1 signaling / LUBAC complex / RBR-type E3 ubiquitin transferase / Antigen processing: Ubiquitination & Proteasome degradation / ubiquitin ligase activator activity / negative regulation of necroptotic process / positive regulation of extrinsic apoptotic signaling pathway ...TNFR1-induced proapoptotic signaling / TNFR1-induced NF-kappa-B signaling pathway / protein linear polyubiquitination / Regulation of TNFR1 signaling / LUBAC complex / RBR-type E3 ubiquitin transferase / Antigen processing: Ubiquitination & Proteasome degradation / ubiquitin ligase activator activity / negative regulation of necroptotic process / positive regulation of extrinsic apoptotic signaling pathway / tumor necrosis factor-mediated signaling pathway / ubiquitin binding / protein kinase C binding / positive regulation of non-canonical NF-kappaB signal transduction / protein polyubiquitination / ubiquitin-protein transferase activity / T cell receptor signaling pathway / double-stranded DNA binding / proteasome-mediated ubiquitin-dependent protein catabolic process / positive regulation of canonical NF-kappaB signal transduction / defense response to bacterium / positive regulation of apoptotic process / positive regulation of transcription by RNA polymerase II / identical protein binding / metal ion binding Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||||||||
![]() | Walinda, E. / Morimoto, D. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Solution structure of the HOIL-1L NZF domain reveals a conformational switch regulating linear ubiquitin affinity. Authors: Walinda, E. / Sugase, K. / Ishii, N. / Shirakawa, M. / Iwai, K. / Morimoto, D. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 203.9 KB | Display | ![]() |
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PDB format | ![]() | 165 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 590.7 KB | Display | ![]() |
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Full document | ![]() | 788.4 KB | Display | |
Data in XML | ![]() | 35 KB | Display | |
Data in CIF | ![]() | 39 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | Similarity search - Function & homology ![]() |
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Other databases |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein | Mass: 7434.277 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: ZN / Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q9WUB0, RBR-type E3 ubiquitin transferase | ||
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#2: Chemical | Has ligand of interest | Y | |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: solution Contents: 1 mM [U-100% 13C; U-100% 15N] HOIL-1L NZF domain, 20 mM HEPES pH 7.0, 1 mM TCEP, 50 mM sodium chloride, 95% H2O/5% D2O Details: NMR sample for structure determination 13C- and 15N-NOESY measurements in isotropic liquid Label: 15N_13C_sample / Solvent system: 95% H2O/5% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | pH: 7.0 / PH err: 0.05 / Pressure: 1013.2 mbar / Temperature: 298 K / Temperature err: 0.2
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-NMR measurement
NMR spectrometer | Type: Bruker AVANCE II / Manufacturer: Bruker / Model: AVANCE II / Field strength: 700 MHz Details: 5-mm 15N/13C/1H z-gradient triple resonance cryogenic probe |
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Processing
NMR software | Name: ![]() |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 |
NMR representative | Selection criteria: closest to the average |
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 250 / Conformers submitted total number: 10 |