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Yorodumi- PDB-5xqm: NMR solution structure of SMO1, Sumo homologue in Caenorhabditis ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 5xqm | ||||||
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| Title | NMR solution structure of SMO1, Sumo homologue in Caenorhabditis elegans | ||||||
Components | Small ubiquitin-related modifier | ||||||
Keywords | SIGNALING PROTEIN / solution structure / Caenorhabditis elegans / Sumo homologue | ||||||
| Function / homology | Function and homology informationpositive regulation of nematode male tail tip morphogenesis / SUMO is conjugated to E1 (UBA2:SAE1) / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / SUMO is proteolytically processed / SUMOylation of transcription factors / SUMOylation of ubiquitinylation proteins / SUMOylation of transcription cofactors / SUMOylation of SUMOylation proteins / SUMOylation of intracellular receptors / SUMOylation of chromatin organization proteins ...positive regulation of nematode male tail tip morphogenesis / SUMO is conjugated to E1 (UBA2:SAE1) / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / SUMO is proteolytically processed / SUMOylation of transcription factors / SUMOylation of ubiquitinylation proteins / SUMOylation of transcription cofactors / SUMOylation of SUMOylation proteins / SUMOylation of intracellular receptors / SUMOylation of chromatin organization proteins / SUMOylation of RNA binding proteins / SUMOylation of DNA replication proteins / Regulation of IFNG signaling / Negative regulation of activity of TFAP2 (AP-2) family transcription factors / Postmitotic nuclear pore complex (NPC) reformation / SUMOylation of nuclear envelope proteins / SUMOylation of DNA damage response and repair proteins / Formation of Incision Complex in GG-NER / multicellular organismal locomotion / nematode larval development / protein localization to chromosome / synaptonemal complex disassembly / mitotic sister chromatid separation / embryo development ending in birth or egg hatching / mitotic metaphase chromosome alignment / muscle cell cellular homeostasis / ubiquitin-like protein ligase binding / protein sumoylation / regulation of protein stability / spindle / protein tag activity / chromosome / regulation of gene expression / negative regulation of DNA-templated transcription / centrosome / negative regulation of transcription by RNA polymerase II / identical protein binding / nucleus / cytoplasm Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Gowda, C.M. / Surana, P. / Das, R. | ||||||
Citation | Journal: PLoS ONE / Year: 2017Title: Structural and functional analysis of SMO-1, the SUMO homolog in Caenorhabditis elegans Authors: Surana, P. / Gowda, C.M. / Tripathi, V. / Broday, L. / Das, R. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 5xqm.cif.gz | 540.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb5xqm.ent.gz | 453.8 KB | Display | PDB format |
| PDBx/mmJSON format | 5xqm.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xq/5xqm ftp://data.pdbj.org/pub/pdb/validation_reports/xq/5xqm | HTTPS FTP |
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-Related structure data
| Similar structure data | |
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| Other databases |
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Links
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Assembly
| Deposited unit | ![]()
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| NMR ensembles |
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Components
| #1: Protein | Mass: 11048.223 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| NMR experiment |
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Sample preparation
| Details | Type: solution Contents: 620 uM [U-13C; U-15N] SMO1, Small Ubiquitin like modifier in C. elegans, 90% H2O/10% D2O Label: 15N-13C_sample / Solvent system: 90% H2O/10% D2O |
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| Sample | Conc.: 620 uM Component: SMO1, Small Ubiquitin like modifier in C. elegans Isotopic labeling: [U-13C; U-15N] |
| Sample conditions | Details: 25mM Phosphate buffer pH6.0, 150mM NaCl / Ionic strength: 150 mM / Label: condition_1 / pH: 6 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
| NMR spectrometer | Type: Bruker AVANCE III / Manufacturer: Bruker / Model: AVANCE III / Field strength: 800 MHz |
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Processing
| NMR software |
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| Refinement | Method: simulated annealing / Software ordinal: 1 Details: WATER REFINEMENT PERFORMED USING PONDEROSA-C/S PACKAGE. | ||||||||||||||||||
| NMR representative | Selection criteria: target function | ||||||||||||||||||
| NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 400 / Conformers submitted total number: 20 |
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