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- PDB-4jgh: Structure of the SOCS2-Elongin BC complex bound to an N-terminal ... -
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Open data
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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 | ||||||
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![]() | LIGASE / Cullin-RING E3 ubiquitin ligases / Ubiquitination / Cytosol | ||||||
Function / homology | ![]() 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 / JAK pathway signal transduction adaptor activity / Inactivation of CSF3 (G-CSF) signaling / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / ERBB2 signaling pathway / Neddylation / Antigen processing: Ubiquitination & Proteasome degradation ...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 / JAK pathway signal transduction adaptor activity / Inactivation of CSF3 (G-CSF) signaling / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / ERBB2 signaling pathway / 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 / 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 / site of DNA damage / cell surface receptor signaling pathway via JAK-STAT / phosphatidylinositol phosphate biosynthetic process / regulation of signal transduction / mammary gland alveolus development / Growth hormone receptor signaling / cellular response to hormone stimulus / Negative regulation of FLT3 / lactation / positive regulation of neuron differentiation / Interleukin-7 signaling / intrinsic apoptotic signaling pathway / transcription corepressor binding / transcription elongation by RNA polymerase II / regulation of cell growth / transcription initiation at RNA polymerase II promoter / Vif-mediated degradation of APOBEC3G / insulin-like growth factor receptor binding / calcium channel activity / Inactivation of CSF3 (G-CSF) signaling / Evasion by RSV of host interferon responses / Downregulation of ERBB2 signaling / G1/S transition of mitotic cell cycle / ubiquitin-protein transferase activity / Antigen processing: Ubiquitination & Proteasome degradation / response to estradiol / protein-macromolecule adaptor activity / Neddylation / signaling receptor activity / ubiquitin-dependent protein catabolic process / transcription regulator complex / transcription coactivator activity / protein ubiquitination / intracellular signal transduction / ubiquitin protein ligase binding / protein-containing complex binding / negative regulation of apoptotic process / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kim, Y.K. / Kwak, M.J. / Ku, B. / Suh, H.Y. / Joo, K. / Lee, J. / Jung, J.U. / Oh, B.H. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 158.1 KB | Display | ![]() |
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PDB format | ![]() | 123.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 447.4 KB | Display | ![]() |
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Full document | ![]() | 470.9 KB | Display | |
Data in XML | ![]() | 28.5 KB | Display | |
Data in CIF | ![]() | 38.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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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.) ![]() ![]() ![]() |
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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.) ![]() ![]() ![]() ![]() |
#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.) ![]() ![]() ![]() ![]() |
#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.) ![]() ![]() ![]() |
Sequence details | THIS DISCREPANC |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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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: ![]() ![]() ![]() |
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 |
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Processing
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Refinement | Method to determine structure: ![]() 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 |