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Yorodumi- PDB-4jgh: Structure of the SOCS2-Elongin BC complex bound to an N-terminal ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4jgh | ||||||
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Title | Structure of the SOCS2-Elongin BC complex bound to an N-terminal fragment of Cullin5 | ||||||
Components |
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Keywords | LIGASE / Cullin-RING E3 ubiquitin ligases / Ubiquitination / Cytosol | ||||||
Function / homology | Function and homology information TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / negative regulation of growth hormone receptor signaling pathway / JAK pathway signal transduction adaptor activity / Inactivation of CSF3 (G-CSF) signaling / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / ERBB2 signaling pathway / reelin-mediated signaling pathway ...TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / negative regulation of growth hormone receptor signaling pathway / JAK pathway signal transduction adaptor activity / Inactivation of CSF3 (G-CSF) signaling / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / ERBB2 signaling pathway / reelin-mediated signaling pathway / phosphorylation-dependent protein binding / regulation of neuron migration / Neddylation / Antigen processing: Ubiquitination & Proteasome degradation / negative regulation of receptor signaling pathway via JAK-STAT / 1-phosphatidylinositol-3-kinase regulator activity / target-directed miRNA degradation / elongin complex / VCB complex / protein K11-linked ubiquitination / phosphatidylinositol 3-kinase complex / growth hormone receptor binding / Cul5-RING ubiquitin ligase complex / growth hormone receptor signaling pathway / SCF ubiquitin ligase complex / Cul2-RING ubiquitin ligase complex / negative regulation of multicellular organism growth / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / ubiquitin ligase complex scaffold activity / site of DNA damage / phosphatidylinositol phosphate biosynthetic process / cell surface receptor signaling pathway via JAK-STAT / regulation of signal transduction / ubiquitin-like ligase-substrate adaptor activity / mammary gland alveolus development / negative regulation of signal transduction / Growth hormone receptor signaling / cellular response to hormone stimulus / insulin-like growth factor receptor binding / Negative regulation of FLT3 / lactation / positive regulation of neuron differentiation / intrinsic apoptotic signaling pathway / Interleukin-7 signaling / transcription corepressor binding / regulation of cell growth / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / Vif-mediated degradation of APOBEC3G / Inactivation of CSF3 (G-CSF) signaling / calcium channel activity / Evasion by RSV of host interferon responses / Downregulation of ERBB2 signaling / ubiquitin-protein transferase activity / G1/S transition of mitotic cell cycle / Antigen processing: Ubiquitination & Proteasome degradation / response to estradiol / signaling receptor activity / Neddylation / protein-macromolecule adaptor activity / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / transcription regulator complex / transcription coactivator activity / intracellular signal transduction / protein ubiquitination / ubiquitin protein ligase binding / protein-containing complex binding / negative regulation of apoptotic process / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å | ||||||
Authors | Kim, Y.K. / Kwak, M.J. / Ku, B. / Suh, H.Y. / Joo, K. / Lee, J. / Jung, J.U. / Oh, B.H. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2013 Title: Structural basis of intersubunit recognition in elongin BC-cullin 5-SOCS box ubiquitin-protein ligase complexes. Authors: Kim, Y.K. / Kwak, M.J. / Ku, B. / Suh, H.Y. / Joo, K. / Lee, J. / Jung, J.U. / Oh, B.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4jgh.cif.gz | 158.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4jgh.ent.gz | 123.8 KB | Display | PDB format |
PDBx/mmJSON format | 4jgh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4jgh_validation.pdf.gz | 447.4 KB | Display | wwPDB validaton report |
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Full document | 4jgh_full_validation.pdf.gz | 470.9 KB | Display | |
Data in XML | 4jgh_validation.xml.gz | 28.5 KB | Display | |
Data in CIF | 4jgh_validation.cif.gz | 38.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jg/4jgh ftp://data.pdbj.org/pub/pdb/validation_reports/jg/4jgh | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 19812.828 Da / Num. of mol.: 1 / Fragment: unp residues 32-198 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CIS2, Homo sapiens, SOCS2, SSI2, STATI2 / Plasmid: pProEx HTa / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O14508 |
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#2: Protein | Mass: 13185.833 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Mus musculus, Tceb2 / Plasmid: pRSFDuet / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P62869 |
#3: Protein | Mass: 10869.457 Da / Num. of mol.: 1 / Fragment: unp residues 17-112 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Mus musculus, Tceb1 / Plasmid: pRSFDuet / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P83940 |
#4: Protein | Mass: 44010.363 Da / Num. of mol.: 1 / Fragment: unp residues 10-386 / Mutation: V341R, L345D Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CUL5, Homo sapiens, VACM1 / Plasmid: pET22b-CPD10H / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)RIPL / References: UniProt: Q93034 |
Sequence details | THIS DISCREPANC |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 5.08 Å3/Da / Density % sol: 75.81 % |
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Crystal grow | Temperature: 295.15 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 0.25 M sodium citrate and 18 % (w/v) PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.15K |
-Data collection
Diffraction | Mean temperature: 77 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-17A / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Feb 18, 2011 |
Radiation | Monochromator: K-B mirror / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3→50 Å / Num. all: 35501 / Num. obs: 34527 / % possible obs: 97.3 % / Observed criterion σ(F): 12.8 / Observed criterion σ(I): 165.9 / Redundancy: 9 % / Net I/σ(I): 23 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2C9W (for SOCS2-Elongin BC) and 2WZK (for Cul5) Resolution: 3→30 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 3→30 Å
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Refine LS restraints |
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LS refinement shell | Highest resolution: 3 Å |