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- PDB-7v8e: Crystal structure of IpaH1.4 LRR domain bound to HOIL-1L UBL domain. -
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Open data
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Basic information
Entry | Database: PDB / ID: 7v8e | ||||||||||||||||||
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Title | Crystal structure of IpaH1.4 LRR domain bound to HOIL-1L UBL domain. | ||||||||||||||||||
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Function / homology | ![]() modulation of process of another organism / protein linear polyubiquitination / LUBAC complex / RBR-type E3 ubiquitin transferase / cytoplasmic sequestering of protein / ubiquitin ligase activator activity / negative regulation of necroptotic process / positive regulation of extrinsic apoptotic signaling pathway / TNFR1-induced proapoptotic signaling / negative regulation of NF-kappaB transcription factor activity ...modulation of process of another organism / protein linear polyubiquitination / LUBAC complex / RBR-type E3 ubiquitin transferase / cytoplasmic sequestering of protein / ubiquitin ligase activator activity / negative regulation of necroptotic process / positive regulation of extrinsic apoptotic signaling pathway / TNFR1-induced proapoptotic signaling / negative regulation of NF-kappaB transcription factor activity / protein sequestering activity / TNFR1-induced NF-kappa-B signaling pathway / ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||||||||||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||||||||
![]() | Liu, J. / Wang, Y. / Pan, L. | ||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Mechanistic insights into the subversion of the linear ubiquitin chain assembly complex by the E3 ligase IpaH1.4 of Shigella flexneri. Authors: Liu, J. / Wang, Y. / Wang, D. / Wang, Y. / Xu, X. / Zhang, Y. / Li, Y. / Zhang, M. / Gong, X. / Tang, Y. / Shen, L. / Li, M. / Pan, L. | ||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 176.2 KB | Display | ![]() |
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PDB format | ![]() | 110 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 7v8fC ![]() 7v8gC ![]() 7v8hC ![]() 4dbgS S: Starting model for refinement C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS ensembles :
NCS oper:
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Components
#1: Protein | Mass: 26991.988 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: M90T / Gene: ipaH1.4 / Production host: ![]() ![]() ![]() References: UniProt: Q9AFJ5, RING-type E3 ubiquitin transferase #2: Protein | Mass: 10183.492 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() References: UniProt: Q9BYM8, RBR-type E3 ubiquitin transferase #3: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 42.09 % |
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Crystal grow![]() | Temperature: 289 K / Method: evaporation / pH: 8.5 Details: 0.2 M (NH4)2SO4, 0.1 M Tris-HCl (pH 8.5), and 25% (w/v) PEG3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Dec 15, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.9→49.38 Å / Num. obs: 47800 / % possible obs: 99.8 % / Redundancy: 6.3 % / Biso Wilson estimate: 34.14 Å2 / CC1/2: 0.998 / Rpim(I) all: 0.025 / Net I/σ(I): 16.3 |
Reflection shell | Resolution: 1.9→1.94 Å / Mean I/σ(I) obs: 2.3 / Num. unique obs: 3094 / CC1/2: 0.765 / Rpim(I) all: 0.283 / % possible all: 99.5 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 4DBG Resolution: 1.9→23.78 Å / SU ML: 0.2683 / Cross valid method: FREE R-VALUE / σ(F): 1.39 / Phase error: 28.1135 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.54 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→23.78 Å
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Refine LS restraints |
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Refine LS restraints NCS |
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LS refinement shell |
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