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- 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 | ||||||
![]() | Small ubiquitin-related modifier | ||||||
![]() | SIGNALING PROTEIN / solution structure / Caenorhabditis elegans / Sumo homologue | ||||||
Function / homology | ![]() 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 DNA damage response and repair proteins / SUMO E3 ligases SUMOylate target proteins / SUMOylation of transcription factors / SUMOylation of ubiquitinylation proteins / SUMOylation of transcription cofactors / SUMOylation of SUMOylation 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 DNA damage response and repair proteins / SUMO E3 ligases SUMOylate target proteins / 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 / Formation of Incision Complex in GG-NER / Regulation of IFNG signaling / Negative regulation of activity of TFAP2 (AP-2) family transcription factors / Postmitotic nuclear pore complex (NPC) reformation / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / multicellular organismal locomotion / nematode larval development / protein localization to chromosome / mitotic sister chromatid separation / synaptonemal complex disassembly / embryo development ending in birth or egg hatching / microtubule organizing center / 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 / negative regulation of transcription by RNA polymerase II / identical protein binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Gowda, C.M. / Surana, P. / Das, R. | ||||||
![]() | ![]() Title: 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. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 540.5 KB | Display | ![]() |
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PDB format | ![]() | 453.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | 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 |