+Open data
-Basic information
Entry | Database: PDB / ID: 2jqz | ||||||
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Title | Solution Structure of the C2 domain of human Smurf2 | ||||||
Components | E3 ubiquitin-protein ligase SMURF2 | ||||||
Keywords | LIGASE / C2 domain / Smurf2 / Ubiquitin protein ligase / Phospholipid binding | ||||||
Function / homology | Function and homology information positive regulation of trophoblast cell migration / regulation of transforming growth factor beta receptor signaling pathway / Signaling by BMP / HECT-type E3 ubiquitin transferase / Wnt signaling pathway, planar cell polarity pathway / SMAD binding / negative regulation of BMP signaling pathway / ubiquitin ligase complex / Downregulation of TGF-beta receptor signaling / Asymmetric localization of PCP proteins ...positive regulation of trophoblast cell migration / regulation of transforming growth factor beta receptor signaling pathway / Signaling by BMP / HECT-type E3 ubiquitin transferase / Wnt signaling pathway, planar cell polarity pathway / SMAD binding / negative regulation of BMP signaling pathway / ubiquitin ligase complex / Downregulation of TGF-beta receptor signaling / Asymmetric localization of PCP proteins / Degradation of AXIN / Downregulation of SMAD2/3:SMAD4 transcriptional activity / negative regulation of transforming growth factor beta receptor signaling pathway / Hedgehog 'on' state / Regulation of RUNX3 expression and activity / ubiquitin-protein transferase activity / positive regulation of canonical Wnt signaling pathway / ubiquitin protein ligase activity / Antigen processing: Ubiquitination & Proteasome degradation / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / protein ubiquitination / Ub-specific processing proteases / nuclear speck / membrane raft / negative regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / nucleoplasm / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics | ||||||
Authors | Wiesner, S. / Ogunjimi, A.A. / Wang, H. / Rotin, D. / Sicheri, F. / Wrana, J.L. / Forman-Kay, J.D. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 2007 Title: Autoinhibition of the HECT-Type Ubiquitin Ligase Smurf2 through Its C2 Domain Authors: Wiesner, S. / Ogunjimi, A.A. / Wang, H.-R. / Rotin, D. / Sicheri, F. / Wrana, J.L. / Forman-Kay, J.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jqz.cif.gz | 889.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jqz.ent.gz | 753.7 KB | Display | PDB format |
PDBx/mmJSON format | 2jqz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jq/2jqz ftp://data.pdbj.org/pub/pdb/validation_reports/jq/2jqz | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 14701.946 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMURF2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): CodonPlus References: UniProt: Q9HAU4, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases) |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 0.2 / pH: 7.2 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing, torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |