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- PDB-2izv: CRYSTAL STRUCTURE OF SOCS-4 IN COMPLEX WITH ELONGIN-B AND ELONGIN... -
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Basic information
Entry | Database: PDB / ID: 2izv | ||||||
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Title | CRYSTAL STRUCTURE OF SOCS-4 IN COMPLEX WITH ELONGIN-B AND ELONGIN-C AT 2.55A RESOLUTION | ||||||
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![]() | TRANSCRIPTION / SIGNAL TRANSDUCTION INHIBITOR / GROWTH REGULATION / SIGNAL TRANSDUCTION / SH2 DOMAIN / NUCLEAR PROTEIN / UBL CONJUGATION PATHWAY / TRANSCRIPTION REGULATION | ||||||
Function / homology | ![]() negative regulation of epidermal growth factor-activated receptor activity / RUNX1 regulates transcription of genes involved in differentiation of keratinocytes / 1-phosphatidylinositol-3-kinase regulator activity / target-directed miRNA degradation / elongin complex / VCB complex / phosphatidylinositol 3-kinase complex / regulation of growth / Cul5-RING ubiquitin ligase complex / Cul2-RING ubiquitin ligase complex ...negative regulation of epidermal growth factor-activated receptor activity / RUNX1 regulates transcription of genes involved in differentiation of keratinocytes / 1-phosphatidylinositol-3-kinase regulator activity / target-directed miRNA degradation / elongin complex / VCB complex / phosphatidylinositol 3-kinase complex / regulation of growth / Cul5-RING ubiquitin ligase complex / Cul2-RING ubiquitin ligase complex / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / phosphatidylinositol phosphate biosynthetic process / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / transcription corepressor binding / transcription initiation at RNA polymerase II promoter / TP53 Regulates Transcription of DNA Repair Genes / transcription elongation by RNA polymerase II / Vif-mediated degradation of APOBEC3G / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Inactivation of CSF3 (G-CSF) signaling / Evasion by RSV of host interferon responses / Regulation of expression of SLITs and ROBOs / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Antigen processing: Ubiquitination & Proteasome degradation / Neddylation / protein-macromolecule adaptor activity / ubiquitin-dependent protein catabolic process / protein-containing complex assembly / intracellular signal transduction / protein ubiquitination / ubiquitin protein ligase binding / regulation of transcription by RNA polymerase II / nucleoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Debreczeni, J.E. / Bullock, A. / Papagrigoriou, E. / Turnbull, A. / Pike, A.C.W. / Gorrec, F. / von Delft, F. / Sundstrom, M. / Arrowsmith, C. / Weigelt, J. ...Debreczeni, J.E. / Bullock, A. / Papagrigoriou, E. / Turnbull, A. / Pike, A.C.W. / Gorrec, F. / von Delft, F. / Sundstrom, M. / Arrowsmith, C. / Weigelt, J. / Edwards, A. / Knapp, S. | ||||||
![]() | ![]() Title: Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box interface and the molecular basis for SOCS-dependent EGFR degradation. Authors: Bullock, A.N. / Rodriguez, M.C. / Debreczeni, J.E. / Songyang, Z. / Knapp, S. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 89.6 KB | Display | ![]() |
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PDB format | ![]() | 66.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2c9wS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 21736.711 Da / Num. of mol.: 1 / Fragment: RESIDUES 274-437 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE ... , 2 types, 2 molecules BC
#2: Protein | Mass: 13147.781 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#3: Protein | Mass: 10974.616 Da / Num. of mol.: 1 / Fragment: RESIDUES 17-112 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Non-polymers , 4 types, 116 molecules ![](data/chem/img/NA.gif)
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#4: Chemical | ChemComp-NA / |
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#5: Chemical | ChemComp-EDO / |
#6: Chemical | ChemComp-CL / |
#7: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.98 Å3/Da / Density % sol: 69 % |
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Crystal grow | Method: vapor diffusion, sitting drop / Details: 150 UL SITTING DROP 2M NACL 10% PEK6K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jun 16, 2006 / Details: MIRRORS |
Radiation | Monochromator: SI 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8984 Å / Relative weight: 1 |
Reflection | Resolution: 2.55→44.68 Å / Num. obs: 19724 / % possible obs: 99.7 % / Observed criterion σ(I): 2 / Redundancy: 2.71 % / Rmerge(I) obs: 0.13 / Net I/σ(I): 9.14 |
Reflection shell | Resolution: 2.55→2.65 Å / Redundancy: 1.72 % / Rmerge(I) obs: 0.36 / Mean I/σ(I) obs: 1.98 / % possible all: 97.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2C9W Resolution: 2.55→77.38 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.911 / SU B: 13.503 / SU ML: 0.152 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.288 / ESU R Free: 0.229 / Stereochemistry target values: MAXIMUM LIKELIHOOD / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 25.83 Å2
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Refinement step | Cycle: LAST / Resolution: 2.55→77.38 Å
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