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Yorodumi- PDB-2asq: Solution Structure of SUMO-1 in Complex with a SUMO-binding Motif... -
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-Basic information
Entry | Database: PDB / ID: 2asq | ||||||
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Title | Solution Structure of SUMO-1 in Complex with a SUMO-binding Motif (SBM) | ||||||
Components |
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Keywords | PROTEIN BINDING / Protein-Peptide Complex / SUMO-1 / Small Ubiquitin-like Modifier 1 / SUMO-Binding Motif / SBM / Protein Inhibitor of Activated STAT / PIASx | ||||||
Function / homology | Function and homology information SUMO ligase activity / negative regulation of transcription by transcription factor localization / SUMOylation of nuclear envelope proteins / Negative regulation of activity of TFAP2 (AP-2) family transcription factors / SUMO is proteolytically processed / negative regulation of delayed rectifier potassium channel activity / SUMO is conjugated to E1 (UBA2:SAE1) / nuclear stress granule / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / negative regulation of androgen receptor signaling pathway ...SUMO ligase activity / negative regulation of transcription by transcription factor localization / SUMOylation of nuclear envelope proteins / Negative regulation of activity of TFAP2 (AP-2) family transcription factors / SUMO is proteolytically processed / negative regulation of delayed rectifier potassium channel activity / SUMO is conjugated to E1 (UBA2:SAE1) / nuclear stress granule / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / negative regulation of androgen receptor signaling pathway / negative regulation of action potential / small protein activating enzyme binding / SUMOylation of DNA methylation proteins / SUMOylation of SUMOylation proteins / SUMOylation of immune response proteins / Maturation of nucleoprotein / Transferases; Acyltransferases; Aminoacyltransferases / SUMOylation of RNA binding proteins / SUMO transferase activity / Postmitotic nuclear pore complex (NPC) reformation / Maturation of nucleoprotein / negative regulation of protein import into nucleus / ubiquitin-specific protease binding / SUMOylation of ubiquitinylation proteins / roof of mouth development / negative regulation of DNA binding / ubiquitin-like protein ligase binding / SUMOylation of DNA replication proteins / protein sumoylation / transcription factor binding / SUMOylation of transcription factors / potassium channel regulator activity / SUMOylation of DNA damage response and repair proteins / nuclear pore / Regulation of IFNG signaling / cellular response to cadmium ion / SUMOylation of chromatin organization proteins / SUMOylation of transcription cofactors / positive regulation of protein-containing complex assembly / transcription coregulator activity / SUMOylation of intracellular receptors / PKR-mediated signaling / negative regulation of DNA-binding transcription factor activity / PML body / protein tag activity / Formation of Incision Complex in GG-NER / Activation of anterior HOX genes in hindbrain development during early embryogenesis / regulation of protein localization / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / cellular response to heat / nuclear membrane / RNA polymerase II-specific DNA-binding transcription factor binding / protein stabilization / nuclear body / nuclear speck / DNA repair / negative regulation of DNA-templated transcription / DNA-templated transcription / ubiquitin protein ligase binding / nucleolus / regulation of transcription by RNA polymerase II / enzyme binding / DNA binding / RNA binding / zinc ion binding / nucleoplasm / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Song, J. / Zhang, Z. / Hu, W. / Chen, Y. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2005 Title: Small Ubiquitin-like Modifier (SUMO) Recognition of a SUMO Binding Motif: A reversal of the bound orientation Authors: Song, J. / Zhang, Z. / Hu, W. / Chen, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2asq.cif.gz | 319.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2asq.ent.gz | 279.1 KB | Display | PDB format |
PDBx/mmJSON format | 2asq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/as/2asq ftp://data.pdbj.org/pub/pdb/validation_reports/as/2asq | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11149.545 Da / Num. of mol.: 1 / Fragment: Structured Region of SUMO-1 (residues 21-97) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SUMO1, SMT3C, SMT3H3, UBL1 / Plasmid: PET11a+ (Novagen) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)(Novagen) / References: UniProt: P63165 |
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#2: Protein/peptide | Mass: 2835.079 Da / Num. of mol.: 1 / Fragment: SUMO-binding Motif in PIASx Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PIAS2, PIASX / Plasmid: PET31a+ / Production host: Escherichia coli (E. coli) / Strain (production host): BLR(DE3)plysS (Novagen) / References: UniProt: O75928 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 10 / Conformers submitted total number: 10 |