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Yorodumi- PDB-6i7r: Structure of pVHL-elongin B-elongin C (VCB) in complex with hydro... -
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-Basic information
Entry | Database: PDB / ID: 6i7r | ||||||
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Title | Structure of pVHL-elongin B-elongin C (VCB) in complex with hydroxylated-HIF-2alpha (523-542) in the P43212 form | ||||||
Components |
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Keywords | GENE REGULATION / E3 UBIQUITIN LIGASE / von Hippel Lindau / Prolyl hydroxylation / HIF / TUMOR SUPPRESSOR / CANCER / PROTEOSOMAL DEGRADATION / UBIQUITIN | ||||||
Function / homology | Function and homology information myoblast fate commitment / Cellular response to hypoxia / regulation of protein neddylation / Transcriptional regulation of pluripotent stem cells / PTK6 Expression / regulation of cellular response to hypoxia / RHOBTB3 ATPase cycle / negative regulation of receptor signaling pathway via JAK-STAT / norepinephrine metabolic process / transcription elongation factor activity ...myoblast fate commitment / Cellular response to hypoxia / regulation of protein neddylation / Transcriptional regulation of pluripotent stem cells / PTK6 Expression / regulation of cellular response to hypoxia / RHOBTB3 ATPase cycle / negative regulation of receptor signaling pathway via JAK-STAT / norepinephrine metabolic process / transcription elongation factor activity / target-directed miRNA degradation / elongin complex / VCB complex / surfactant homeostasis / epithelial cell maturation / Replication of the SARS-CoV-1 genome / Cul5-RING ubiquitin ligase complex / Regulation of gene expression by Hypoxia-inducible Factor / Cul2-RING ubiquitin ligase complex / intracellular non-membrane-bounded organelle / SUMOylation of ubiquitinylation proteins / negative regulation of transcription elongation by RNA polymerase II / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / ubiquitin-like ligase-substrate adaptor activity / embryonic placenta development / Tat-mediated elongation of the HIV-1 transcript / blood vessel remodeling / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / negative regulation of signal transduction / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / negative regulation of TORC1 signaling / RNA Polymerase II Pre-transcription Events / visual perception / Pexophagy / regulation of heart rate / negative regulation of autophagy / transcription corepressor binding / erythrocyte differentiation / mitochondrion organization / transcription initiation at RNA polymerase II promoter / TP53 Regulates Transcription of DNA Repair Genes / positive regulation of cell differentiation / RNA polymerase II transcription regulatory region sequence-specific DNA binding / transcription elongation by RNA polymerase II / Vif-mediated degradation of APOBEC3G / lung development / mRNA transcription by RNA polymerase II / cell morphogenesis / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Inactivation of CSF3 (G-CSF) signaling / Evasion by RSV of host interferon responses / transcription coactivator binding / multicellular organismal-level iron ion homeostasis / Regulation of expression of SLITs and ROBOs / ubiquitin-protein transferase activity / transcription corepressor activity / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Antigen processing: Ubiquitination & Proteasome degradation / Neddylation / positive regulation of cold-induced thermogenesis / protein-macromolecule adaptor activity / Replication of the SARS-CoV-2 genome / cellular response to hypoxia / ubiquitin-dependent protein catabolic process / regulation of gene expression / protein-containing complex assembly / DNA-binding transcription activator activity, RNA polymerase II-specific / proteasome-mediated ubiquitin-dependent protein catabolic process / angiogenesis / DNA-binding transcription factor binding / RNA polymerase II-specific DNA-binding transcription factor binding / response to oxidative stress / transcription regulator complex / amyloid fibril formation / molecular adaptor activity / response to hypoxia / protein stabilization / DNA-binding transcription factor activity, RNA polymerase II-specific / protein ubiquitination / nuclear speck / protein heterodimerization activity / RNA polymerase II cis-regulatory region sequence-specific DNA binding / negative regulation of cell population proliferation / negative regulation of gene expression / ubiquitin protein ligase binding / regulation of DNA-templated transcription / chromatin / regulation of transcription by RNA polymerase II / negative regulation of apoptotic process / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / enzyme binding / signal transduction / endoplasmic reticulum / positive regulation of transcription by RNA polymerase II Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.949 Å | ||||||
Authors | Chowdhury, R. / Aguilera, L.S. / Schofield, C.J. | ||||||
Citation | Journal: To Be Published Title: HIF-2alpha-pVHL-elongin B-elongin C complex Authors: Chowdhury, R. / Schofield, C.J. #1: Journal: Nature / Year: 2002 Title: Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL. Authors: Hon, W.C. / Wilson, M.I. / Harlos, K. / Claridge, T.D. / Schofield, C.J. / Pugh, C.W. / Maxwell, P.H. / Ratcliffe, P.J. / Stuart, D.I. / Jones, E.Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6i7r.cif.gz | 236 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6i7r.ent.gz | 191.9 KB | Display | PDB format |
PDBx/mmJSON format | 6i7r.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i7/6i7r ftp://data.pdbj.org/pub/pdb/validation_reports/i7/6i7r | HTTPS FTP |
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-Related structure data
Related structure data | 6i7qC 1lqbS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein , 3 types, 3 molecules BCV
#1: Protein | Mass: 13259.844 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ELOB, TCEB2 / Plasmid: PLASMID / Details (production host): pGEX-4T-3 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q15370 |
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#2: Protein | Mass: 10957.523 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ELOC, TCEB1 / Plasmid: PLASMID / Details (production host): pBB75 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q15369 |
#4: Protein | Mass: 18558.162 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: VHL / Plasmid: PLASMID / Details (production host): pGEX-4T-3 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P40337 |
-Protein/peptide , 1 types, 1 molecules H
#3: Protein/peptide | Mass: 2315.529 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q99814 |
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-Non-polymers , 2 types, 396 molecules
#5: Chemical | ChemComp-FMT / |
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#6: 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: 2.74 Å3/Da / Density % sol: 55.14 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 5.8 Details: 0.1M Cacodyl-Na pH 5.8, 0.1M Mg Formate, 50mM Cystamine, 22% PEG3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9795 Å |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Oct 3, 2017 / Details: MIRRORS |
Radiation | Monochromator: SI 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 1.949→262.01 Å / Num. obs: 38067 / % possible obs: 100 % / Redundancy: 24.9 % / Biso Wilson estimate: 28.5 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.175 / Rpim(I) all: 0.035 / Rrim(I) all: 0.178 / Net I/σ(I): 14 |
Reflection shell | Resolution: 1.949→2.06 Å / Redundancy: 25.2 % / Rmerge(I) obs: 1.945 / Mean I/σ(I) obs: 2 / Num. unique obs: 5457 / CC1/2: 0.727 / Rpim(I) all: 0.393 / Rrim(I) all: 1.985 / % possible all: 100 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1LQB Resolution: 1.949→65.454 Å / SU ML: 0.18 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 18.85
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Bsol: 52.7 Å2 / ksol: 0.38 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 41 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.949→65.454 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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