+Open data
-Basic information
Entry | Database: PDB / ID: 5git | ||||||
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Title | BTB domain of KEAP1 in complex with XX3 | ||||||
Components | Kelch-like ECH-associated protein 1 | ||||||
Keywords | TRANSCRIPTION / SIGNALING PROTEIN | ||||||
Function / homology | Function and homology information regulation of epidermal cell differentiation / Nuclear events mediated by NFE2L2 / Cul3-RING ubiquitin ligase complex / ubiquitin-like ligase-substrate adaptor activity / centriolar satellite / inclusion body / cellular response to interleukin-4 / regulation of autophagy / actin filament / negative regulation of DNA-binding transcription factor activity ...regulation of epidermal cell differentiation / Nuclear events mediated by NFE2L2 / Cul3-RING ubiquitin ligase complex / ubiquitin-like ligase-substrate adaptor activity / centriolar satellite / inclusion body / cellular response to interleukin-4 / regulation of autophagy / actin filament / negative regulation of DNA-binding transcription factor activity / KEAP1-NFE2L2 pathway / disordered domain specific binding / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Antigen processing: Ubiquitination & Proteasome degradation / cellular response to oxidative stress / Neddylation / midbody / ubiquitin-dependent protein catabolic process / in utero embryonic development / RNA polymerase II-specific DNA-binding transcription factor binding / Potential therapeutics for SARS / protein ubiquitination / Ub-specific processing proteases / endoplasmic reticulum / nucleoplasm / identical protein binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.19 Å | ||||||
Authors | Zhu, L.L. / Li, H.L. / Wu, F.S. / Xiong, R. | ||||||
Citation | Journal: Antioxid. Redox Signal. / Year: 2017 Title: Britanin Ameliorates Cerebral Ischemia-Reperfusion Injury by Inducing the Nrf2 Protective Pathway. Authors: Wu, G.Z. / Zhu, L.L. / Yuan, X. / Chen, H. / Xiong, R. / Zhang, S.D. / Cheng, H. / Shen, Y.H. / An, H.Z. / Li, T.J. / Li, H.L. / Zhang, W.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5git.cif.gz | 37.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5git.ent.gz | 27.4 KB | Display | PDB format |
PDBx/mmJSON format | 5git.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gi/5git ftp://data.pdbj.org/pub/pdb/validation_reports/gi/5git | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 15293.651 Da / Num. of mol.: 1 / Fragment: BTB, UNP residues 48-180 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KEAP1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q14145 |
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#2: Chemical | ChemComp-XXT / [( |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45.45 % |
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Crystal grow | Temperature: 293 K / Method: evaporation / Details: 0.2 M lithium acetate, 16% PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.987 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 19, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.987 Å / Relative weight: 1 |
Reflection | Resolution: 2.19→36.76 Å / Num. obs: 8098 / % possible obs: 99.5 % / Redundancy: 11.8 % / Net I/σ(I): 17.2 |
-Processing
Software |
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Refinement | Resolution: 2.19→36.76 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.919 / SU B: 6.833 / SU ML: 0.174 / Cross valid method: THROUGHOUT / ESU R: 0.274 / ESU R Free: 0.233 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 58.168 Å2
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Refinement step | Cycle: 1 / Resolution: 2.19→36.76 Å
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Refine LS restraints |
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